| Year |
Citation |
Score |
| 2020 |
Soldatova AV, Spiro TG. Alternative modes of O activation in P450 and NOS enzymes are clarified by DFT modeling and resonance Raman spectroscopy. Journal of Inorganic Biochemistry. 207: 111054. PMID 32217351 DOI: 10.1016/J.Jinorgbio.2020.111054 |
0.322 |
|
| 2019 |
Tang L, Zhu L, Ener ME, Gao H, Wang Y, Groves JT, Spiro TG, Fang C. Photoinduced charge flow inside an iron porphyrazine complex. Chemical Communications (Cambridge, England). PMID 31657387 DOI: 10.1039/C9Cc06193B |
0.336 |
|
| 2019 |
Deng H, Ke S, Callender R, Balakrishnan G, Spiro TG, May ER, Brooks CL. Computational Studies of Catalytic Loop Dynamics in Protein Tyrosine Phosphatase Using Pathway Optimization Methods. The Journal of Physical Chemistry. B. PMID 31437399 DOI: 10.1021/Acs.Jpcb.9B06759 |
0.347 |
|
| 2019 |
Soldatova AV, Balakrishnan G, Oyerinde OF, Romano C, Tebo BM, Spiro TG. Biogenic and synthetic MnO nanoparticles: size and growth probed with absorption and Raman spectroscopies and dynamic light scattering. Environmental Science & Technology. PMID 30905145 DOI: 10.1021/Acs.Est.8B05806 |
0.329 |
|
| 2018 |
Tao L, Stich TA, Soldatova AV, Tebo BM, Spiro TG, Casey WH, Britt RD. Mn(III) species formed by the multi-copper oxidase MnxG investigated by electron paramagnetic resonance spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 29968177 DOI: 10.1007/S00775-018-1587-Z |
0.356 |
|
| 2018 |
Vaughn MB, Zhang J, Spiro TG, Dyer RB, Klinman JP. Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase. Journal of the American Chemical Society. PMID 29323490 DOI: 10.1021/Jacs.7B12369 |
0.484 |
|
| 2017 |
Tao L, Stich TA, Liou SH, Soldatova AV, Delgadillo DA, Romano CA, Spiro TG, Goodin DB, Tebo BM, Casey WH, Britt RD. Copper Binding Sites in the Manganese-Oxidizing Mnx Protein Complex Investigated by Electron Paramagnetic Resonance Spectroscopy. Journal of the American Chemical Society. PMID 28587464 DOI: 10.1021/Jacs.7B02277 |
0.307 |
|
| 2015 |
Butterfield CN, Tao L, Chacón KN, Spiro TG, Blackburn NJ, Casey WH, Britt RD, Tebo BM. Multicopper manganese oxidase accessory proteins bind Cu and heme. Biochimica Et Biophysica Acta. 1854: 1853-9. PMID 26327317 DOI: 10.1016/J.Bbapap.2015.08.012 |
0.315 |
|
| 2015 |
Tao L, Stich TA, Butterfield CN, Romano CA, Spiro TG, Tebo BM, Casey WH, Britt RD. Mn(II) Binding and Subsequent Oxidation by the Multicopper Oxidase MnxG Investigated by Electron Paramagnetic Resonance Spectroscopy. Journal of the American Chemical Society. 137: 10563-75. PMID 26244911 DOI: 10.1021/Jacs.5B04331 |
0.334 |
|
| 2014 |
Jones EM, Monza E, Balakrishnan G, Blouin GC, Mak PJ, Zhu Q, Kincaid JR, Guallar V, Spiro TG. Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study. Journal of the American Chemical Society. 136: 10325-39. PMID 24991732 DOI: 10.1021/Ja503328A |
0.326 |
|
| 2014 |
Jones EM, Balakrishnan G, Squier TC, Spiro TG. Distinguishing unfolding and functional conformational transitions of calmodulin using ultraviolet resonance Raman spectroscopy Protein Science. 23: 1094-1101. PMID 24895328 DOI: 10.1002/Pro.2495 |
0.382 |
|
| 2014 |
Balakrishnan G, Soldatova AV, Reid PJ, Spiro TG. Ultrafast charge transfer in nickel phthalocyanine probed by femtosecond Raman-induced kerr effect spectroscopy Journal of the American Chemical Society. 136: 8746-8754. PMID 24841906 DOI: 10.1021/Ja503541V |
0.3 |
|
| 2013 |
Soldatova AV, Ibrahim M, Spiro TG. Electronic structure and ligand vibrations in FeNO, CoNO, and FeOO porphyrin adducts Inorganic Chemistry. 52: 7478-7486. PMID 23763617 DOI: 10.1021/Ic400364X |
0.336 |
|
| 2013 |
Spiro TG, Soldatova AV, Balakrishnan G. CO, NO and O2 as Vibrational Probes of Heme Protein Interactions. Coordination Chemistry Reviews. 257: 511-527. PMID 23471138 DOI: 10.1016/J.Ccr.2012.05.008 |
0.395 |
|
| 2012 |
Balakrishnan G, Hu Y, Spiro TG. His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: Implications for apoptosis Journal of the American Chemical Society. 134: 19061-19069. PMID 23094892 DOI: 10.1021/Ja307100A |
0.373 |
|
| 2012 |
Spiro TG, Soldatova AV. Ambidentate H-bonding of NO and O2 in heme proteins Journal of Inorganic Biochemistry. 115: 204-210. PMID 22824153 DOI: 10.1016/J.Jinorgbio.2012.05.013 |
0.329 |
|
| 2012 |
Balakrishnan G, Jarzecki AA, Wu Q, Kozlowski PM, Wang D, Spiro TG. Mode recognition in UV resonance Raman spectra of imidazole: histidine monitoring in proteins. The Journal of Physical Chemistry. B. 116: 9387-95. PMID 22779777 DOI: 10.1021/Jp305083T |
0.658 |
|
| 2012 |
Jones EM, Balakrishnan G, Spiro TG. Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: A resonance Raman spectroscopic study Journal of the American Chemical Society. 134: 3461-3471. PMID 22263778 DOI: 10.1021/Ja210126J |
0.371 |
|
| 2012 |
Li XY, Spiro TG. Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data. Journal of the American Chemical Society. 110: 6024-33. PMID 22148777 DOI: 10.1021/Ja00226A017 |
0.413 |
|
| 2012 |
Balakrishnan G, Jarzecki AA, Wu Q, Kozlowski PM, Wang D, Spiro TG. Mode recognition in UV resonance Raman spectra of imidazole: Histidine monitoring in proteins Journal of Physical Chemistry B. 116: 9387-9395. DOI: 10.1021/jp305083t |
0.59 |
|
| 2012 |
Weeks CL, Jo H, Kier B, De Grado WF, Spiro TG. Cysteine-linked aromatic nitriles as UV resonance Raman probes of protein structure Journal of Raman Spectroscopy. 43: 1244-1249. DOI: 10.1002/Jrs.3167 |
0.454 |
|
| 2010 |
Ibrahim M, Derbyshire ER, Soldatova AV, Marletta MA, Spiro TG. Soluble guanylate cyclase is activated differently by excess NO and by YC-1: resonance Raman spectroscopic evidence. Biochemistry. 49: 4864-71. PMID 20459051 DOI: 10.1021/Bi100506J |
0.425 |
|
| 2010 |
Ibrahim M, Derbyshire ER, Marletta MA, Spiro TG. Probing soluble guanylate cyclase activation by CO and YC-1 using resonance Raman spectroscopy. Biochemistry. 49: 3815-23. PMID 20353168 DOI: 10.1021/Bi902214J |
0.429 |
|
| 2010 |
Soldatova AV, Ibrahim M, Olson JS, Czernuszewicz RS, Spiro TG. New light on NO bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling. Journal of the American Chemical Society. 132: 4614-25. PMID 20218710 DOI: 10.1021/Ja906233M |
0.395 |
|
| 2009 |
Weeks CL, Singh S, Madzelan P, Banerjee R, Spiro TG. Heme regulation of human cystathionine β-synthase activity: Insights from fluorescence and Raman spectroscopy Journal of the American Chemical Society. 131: 12809-12816. PMID 19722721 DOI: 10.1021/Ja904468W |
0.388 |
|
| 2009 |
Balakrishnan G, Ibrahim M, Mak PJ, Hata J, Kincaid JR, Spiro TG. Linking conformation change to hemoglobin activation via chain-selective time-resolved resonance Raman spectroscopy of protoheme/mesoheme hybrids Journal of Biological Inorganic Chemistry. 14: 741-750. PMID 19288145 DOI: 10.1007/S00775-009-0487-7 |
0.38 |
|
| 2009 |
Balakrishnan G, Zhao X, Podstawska E, Proniewicz LM, Kincaid JR, Spiro TG. Subunit-selective interrogation of CO recombination in carbonmonoxy hemoglobin by isotope-edited time-resolved resonance Raman spectroscopy Biochemistry. 48: 3120-3126. PMID 19245215 DOI: 10.1021/Bi802190F |
0.363 |
|
| 2009 |
Singh S, Madzelan P, Stasser J, Weeks CL, Becker D, Spiro TG, Penner-Hahn J, Banerjee R. Modulation of the heme electronic structure and cystathionine β-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation Journal of Inorganic Biochemistry. 103: 689-697. PMID 19232736 DOI: 10.1016/J.Jinorgbio.2009.01.009 |
0.342 |
|
| 2009 |
Duckworth OW, Bargar JR, Jarzecki AA, Oyerinde O, Spiro TG, Sposito G. The exceptionally stable cobalt(III)-desferrioxamine B complex Marine Chemistry. 113: 114-122. DOI: 10.1016/J.Marchem.2009.01.003 |
0.322 |
|
| 2009 |
Balakrishnan G, Ibrahim M, Mak PJ, Hata J, Kincaid JR, Spiro TG. Linking Heme Activation to Conformation Change in Hemoglobin Via Chain Selective Time-resolved Resonance Raman Spectroscopy on Mesoheme Hybrids Biophysical Journal. 96: 435a-436a. DOI: 10.1016/J.Bpj.2008.12.2233 |
0.383 |
|
| 2008 |
Weeks CL, Polishchuk A, Getahun Z, Degrado WF, Spiro TG. Investigation of an unnatural amino acid for use as a resonance Raman probe: Detection limits, solvent and temperature dependence of the νC≡N band of 4-cyanophenylalanine. Journal of Raman Spectroscopy : Jrs. 39: 1606-1613. PMID 20648227 DOI: 10.1002/Jrs.2067 |
0.455 |
|
| 2008 |
Balakrishnan G, Weeks CL, Ibrahim M, Soldatova AV, Spiro TG. Protein dynamics from time resolved UV Raman spectroscopy Current Opinion in Structural Biology. 18: 623-629. PMID 18606227 DOI: 10.1016/J.Sbi.2008.06.001 |
0.371 |
|
| 2008 |
Derbyshire ER, Gunn A, Ibrahim M, Spiro TG, Britt RD, Marletta MA. Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes. Biochemistry. 47: 3892-9. PMID 18302323 DOI: 10.1021/Bi7022943 |
0.346 |
|
| 2008 |
Xu C, Spiro TG. Ambidentate H-bonding by heme-bound NO: Structural and spectral effects of -O versus -N H-bonding Journal of Biological Inorganic Chemistry. 13: 613-621. PMID 18274790 DOI: 10.1007/S00775-008-0349-8 |
0.534 |
|
| 2008 |
Xu C, Ibrahim M, Spiro TG. DFT analysis of axial and equatorial effects on heme-CO vibrational modes: Applications to CooA and H-NOX heme sensor proteins Biochemistry. 47: 2379-2387. PMID 18217776 DOI: 10.1021/Bi702254Y |
0.548 |
|
| 2008 |
Oyerinde OF, Weeks CL, Anbar AD, Spiro TG. Solution structure of molybdic acid from Raman spectroscopy and DFT analysis Inorganica Chimica Acta. 361: 1000-1007. DOI: 10.1016/J.Ica.2007.06.025 |
0.385 |
|
| 2007 |
Alcantara RE, Xu C, Spiro TG, Guallar V. A quantum-chemical picture of hemoglobin affinity Proceedings of the National Academy of Sciences of the United States of America. 104: 18451-18455. PMID 18003918 DOI: 10.1073/Pnas.0706026104 |
0.499 |
|
| 2007 |
Spiro TG. Adventures in bioinorganic chemistry Inorganic Chemistry. 46: 10968-10980. PMID 17999486 DOI: 10.1021/Ic700555Y |
0.347 |
|
| 2007 |
Balakrishnan G, Hu Y, Bender GM, Getahun Z, DeGrado WF, Spiro TG. Enthalpic and entropic stages in alpha-helical peptide unfolding, from laser T-jump/UV Raman spectroscopy. Journal of the American Chemical Society. 129: 12801-8. PMID 17910449 DOI: 10.1021/Ja073366L |
0.372 |
|
| 2007 |
Jin N, Ibrahim M, Spiro TG, Groves JT. Trans-dioxo manganese(V) porphyrins. Journal of the American Chemical Society. 129: 12416-7. PMID 17887684 DOI: 10.1021/Ja0761737 |
0.409 |
|
| 2007 |
Ibrahim M, Kuchinskas M, Youn H, Kerby RL, Roberts GP, Poulos TL, Spiro TG. Mechanism of the CO-sensing heme protein CooA: New insights from the truncated heme domain and UVRR spectroscopy Journal of Inorganic Biochemistry. 101: 1776-1785. PMID 17720248 DOI: 10.1016/J.Jinorgbio.2007.07.010 |
0.326 |
|
| 2007 |
Balakrishnan G, Hu Y, Oyerinde OF, Su J, Groves JT, Spiro TG. A conformational switch to β-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis Journal of the American Chemical Society. 129: 504-505. PMID 17227009 DOI: 10.1021/Ja0678727 |
0.361 |
|
| 2006 |
Ibrahim M, Xu C, Spiro TG. Differential sensing of protein influences by NO and CO vibrations in heme adducts Journal of the American Chemical Society. 128: 16834-16845. PMID 17177434 DOI: 10.1021/Ja064859D |
0.599 |
|
| 2006 |
Balakrishnan G, Hu Y, Case MA, Spiro TG. Microsecond melting of a folding intermediate in a coiled-coil peptide, monitored by T-jump/UV Raman spectroscopy. The Journal of Physical Chemistry. B. 110: 19877-83. PMID 17020373 DOI: 10.1021/Jp061987F |
0.366 |
|
| 2006 |
Ibrahim M, Kerby RL, Puranik M, Wasbotten IH, Youn H, Roberts GP, Spiro TG. Heme displacement mechanism of CooA activation: Mutational and Raman spectroscopic evidence Journal of Biological Chemistry. 281: 29165-29173. PMID 16873369 DOI: 10.1074/Jbc.M605568200 |
0.736 |
|
| 2006 |
Kozlowski PM, Andruniow T, Jarzecki AA, Zgierski MZ, Spiro TG. DFT analysis of co-alkyl and co-adenosyl vibrational modes in B 12-cofactors Inorganic Chemistry. 45: 5585-5590. PMID 16813422 DOI: 10.1021/Ic052069J |
0.635 |
|
| 2006 |
Balakrishnan G, Ying H, Spiro TG. Temperature-jump apparatus with Raman detection based on a solid-state tunable (1.80-2.05 μm) kHz optical parametric oscillator laser Applied Spectroscopy. 60: 347-351. PMID 16613628 DOI: 10.1366/000370206776593799 |
0.322 |
|
| 2006 |
Stich TA, Seravalli J, Venkateshrao S, Spiro TG, Ragsdale SW, Brunold TC. Spectroscopic studies of the corrinoid/iron-sulfur protein from Moorella thermoacetica. Journal of the American Chemical Society. 128: 5010-20. PMID 16608335 DOI: 10.1021/Ja054690O |
0.341 |
|
| 2006 |
Puranik M, Weeks CL, Lahaye D, Kabil O, Taoka S, Nielsen SB, Groves JT, Banerjee R, Spiro TG. Dynamics of carbon monoxide binding to cystathionine βsynthase Journal of Biological Chemistry. 281: 13433-13438. PMID 16505479 DOI: 10.1074/Jbc.M600246200 |
0.714 |
|
| 2006 |
Jiji RD, Balakrishnan G, Hu Y, Spiro TG. Intermediacy of Poly(L-proline) II and β-strand conformations in poly(L-lysine) β-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy Biochemistry. 45: 34-41. PMID 16388578 DOI: 10.1021/Bi051507V |
0.33 |
|
| 2006 |
Kneipp J, Balakrishnan G, Chen R, Shen TJ, Sahu SC, Ho NT, Giovannelli JL, Simplaceanu V, Ho C, Spiro TG. Dynamics of allostery in hemoglobin: roles of the penultimate tyrosine H bonds. Journal of Molecular Biology. 356: 335-53. PMID 16368110 DOI: 10.1016/J.Jmb.2005.11.006 |
0.653 |
|
| 2006 |
Huang CY, Balakrishnan G, Spiro TG. Protein secondary structure from deep-UV resonance Raman spectroscopy Journal of Raman Spectroscopy. 37: 277-282. DOI: 10.1002/Jrs.1440 |
0.425 |
|
| 2005 |
De Angelis F, Jarzecki AA, Car R, Spiro TG. Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin. The Journal of Physical Chemistry. B. 109: 3065-70. PMID 16851321 DOI: 10.1021/Jp0451851 |
0.311 |
|
| 2005 |
Jarz?cki AA, Spiro TG. Porphyrin distortion from resonance Raman intensities of out-of-plane modes: Computation and modeling of N-methylmesoporphyrin, a ferrochelatase transition state analog Journal of Physical Chemistry A. 109: 421-430. PMID 16833362 DOI: 10.1021/Jp0470142 |
0.399 |
|
| 2005 |
Horsman GP, Jirasek A, Vaillancourt FH, Barbosa CJ, Jarzecki AA, Xu C, Mekmouche Y, Spiro TG, Lipscomb JD, Blades MW, Turner RF, Eltis LD. Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenase. Journal of the American Chemical Society. 127: 16882-91. PMID 16316234 DOI: 10.1021/Ja053800O |
0.6 |
|
| 2005 |
Huang CY, Balakrishnan G, Spiro TG. Early events in apomyoglobin unfolding probed by laser T-jump/UV resonance raman spectroscopy Biochemistry. 44: 15734-15742. PMID 16313176 DOI: 10.1021/Bi051578U |
0.369 |
|
| 2005 |
Balakrishnan G, Hu Y, Nielsen SB, Spiro TG. Tunable kHz deep ultraviolet (193-210 nm) laser for Raman applications Applied Spectroscopy. 59: 776-781. PMID 16053544 DOI: 10.1366/0003702054280702 |
0.335 |
|
| 2005 |
Spiro TG, Wasbotten IH. CO as a vibrational probe of heme protein active sites Journal of Inorganic Biochemistry. 99: 34-44. PMID 15598489 DOI: 10.1016/J.Jinorgbio.2004.09.026 |
0.402 |
|
| 2005 |
Edwards DC, Nielsen SB, Jarzecki AA, Spiro TG, Myneni SCB. Experimental and theoretical vibrational spectroscopy studies of acetohydroxamic acid and desferrioxamine B in aqueous solution: Effects of pH and iron complexation Geochimica Et Cosmochimica Acta. 69: 3237-3248. DOI: 10.1016/J.Gca.2005.01.030 |
0.577 |
|
| 2005 |
Anbar AD, Jarzecki AA, Spiro TG. Theoretical investigation of iron isotope fractionation between Fe(H2O)6 3+ and Fe(H2O) 6 2+: Implications for iron stable isotope geochemistry Geochimica Et Cosmochimica Acta. 69: 825-837. DOI: 10.1016/J.Gca.2004.06.012 |
0.323 |
|
| 2004 |
Venkateshrao S, Yin J, Jarzecki AA, Schultz PG, Spiro TG. Porphyrin distortion during affinity maturation of a ferrochelatase antibody, monitored by Resonance Raman spectroscopy. Journal of the American Chemical Society. 126: 16361-7. PMID 15600337 DOI: 10.1021/Ja0465395 |
0.386 |
|
| 2004 |
Balakrishnan G, Tsai CH, Wu Q, Case MA, Pevsner A, McLendon GL, Ho C, Spiro TG. Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: Time-resolved UV resonance raman evidence for intra-dimer coupling Journal of Molecular Biology. 340: 857-868. PMID 15223326 DOI: 10.1016/J.Jmb.2004.05.013 |
0.329 |
|
| 2004 |
Balakrishnan G, Case MA, Pevsner A, Zhao X, Tengroth C, McLendon GL, Spiro TG. Time-resolved absorption and UV resonance raman spectra reveal stepwise formation of T quaternary contacts in the allosteric pathway of hemoglobin Journal of Molecular Biology. 340: 843-856. PMID 15223325 DOI: 10.1016/J.Jmb.2004.05.012 |
0.393 |
|
| 2004 |
Puranik M, Nielsen SB, Youn H, Hvitved AN, Bourassa JL, Case MA, Tengroth C, Balakrishnan G, Thorsteinsson MV, Groves JT, McLendon GL, Roberts GP, Olson JS, Spiro TG. Dynamics of carbon monoxide binding to CooA. The Journal of Biological Chemistry. 279: 21096-108. PMID 14990568 DOI: 10.1074/Jbc.M400613200 |
0.696 |
|
| 2004 |
Kneipp J, Balakrishnan G, Spiro TG. Time-resolved resonance raman study of HbA with 220 nm excitation: Probing phenylalanine Journal of Physical Chemistry B. 108: 15919-15927. DOI: 10.1021/Jp047848K |
0.402 |
|
| 2004 |
Jarzecki AA, Anbar AD, Spiro TG. DFT Analysis of Fe(H2O)3+6 and Fe(H2O)2+6 Structure and Vibrations; Implications for Isotope Fractionation. Cheminform. 35. DOI: 10.1021/Jp036418B |
0.337 |
|
| 2003 |
Wang Y, Spiro TG. Vibrational and electronic couplings in ultraviolet resonance Raman spectra of cyclic peptides Biophysical Chemistry. 105: 461-470. PMID 14499911 DOI: 10.1016/S0301-4622(03)00108-X |
0.425 |
|
| 2003 |
Coyle CM, Puranik M, Youn H, Brøndsted Nielsen S, Williams RD, Kerby RL, Roberts GP, Spiro TG. Activation mechanism of the CO sensor CooA: Mutational and resonance Raman spectroscopic studies Journal of Biological Chemistry. 278: 35384-35393. PMID 12796503 DOI: 10.1074/Jbc.M301000200 |
0.742 |
|
| 2003 |
Coyle CM, Vogel KM, Rush TS, Kozlowski PM, Williams R, Spiro TG, Dou Y, Ikeda-Saito M, Olson JS, Zgierski MZ. FeNO structure in distal pocket mutants of myoglobin based on resonance Raman spectroscopy. Biochemistry. 42: 4896-903. PMID 12718530 DOI: 10.1021/Bi026395B |
0.631 |
|
| 2003 |
Tsai CH, Simplaceanu V, Ho NT, Shen TJ, Wang D, Spiro TG, Ho C. Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the free energies of oxygenation. Biophysical Chemistry. 100: 131-42. PMID 12646359 DOI: 10.1016/S0301-4622(02)00274-0 |
0.317 |
|
| 2003 |
Wu Q, Balakrishnan G, Pevsner A, Spiro TG. Histidine photodegradation during UV resonance Raman spectroscopy Journal of Physical Chemistry A. 107: 8047-8051. DOI: 10.1021/Jp027190F |
0.405 |
|
| 2002 |
Maliekal J, Karapetian A, Vance C, Yikilmaz E, Wu Q, Jackson T, Brunold TC, Spiro TG, Miller AF. Comparison and contrasts between the active site PKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase. Journal of the American Chemical Society. 124: 15064-75. PMID 12475351 DOI: 10.1021/Ja027319Z |
0.309 |
|
| 2002 |
Carr HS, Tran D, Reynolds MF, Burstyn JN, Spiro TG. Activation of soluble guanylyl cyclase by four-coordinate metalloporphyrins: evidence for a role for porphyrin conformation. Biochemistry. 41: 10149-57. PMID 12146980 DOI: 10.1021/Bi010777K |
0.347 |
|
| 2002 |
Wu Q, Li F, Wang W, Hecht MH, Spiro TG. UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin. Journal of Inorganic Biochemistry. 88: 381-7. PMID 11897354 DOI: 10.1016/S0162-0134(01)00354-3 |
0.378 |
|
| 2002 |
Vaillancourt FH, Barbosa CJ, Spiro TG, Bolin JT, Blades MW, Turner RFB, Eltis LD. Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography Journal of the American Chemical Society. 124: 2485-2496. PMID 11890797 DOI: 10.1021/Ja0174682 |
0.432 |
|
| 2002 |
Chen R, Spiro TG. Monitoring the allosteric transition and CO rebinding in hemoglobin with time-resolved FTIR spectroscopy Journal of Physical Chemistry A. 106: 3413-3419. DOI: 10.1021/Jp012491V |
0.651 |
|
| 2001 |
Moffet DA, Case MA, House JC, Vogel K, Williams RD, Spiro TG, McLendon GL, Hecht MH. Carbon monoxide binding by de novo heme proteins derived from designed combinatorial libraries. Journal of the American Chemical Society. 123: 2109-15. PMID 11456855 DOI: 10.1021/Ja0036007 |
0.333 |
|
| 2001 |
Zhao X, Chen R, Raj V, Spiro TG. Assignment of the 1511 cm(-1) UV resonance Raman marker band of hemoglobin to tryptophan. Biopolymers. 62: 158-62. PMID 11343285 DOI: 10.1002/Bip.1009 |
0.66 |
|
| 2001 |
Spiro TG, Kozlowski PM. Is the CO adduct of myoglobin bent, and does it matter? Accounts of Chemical Research. 34: 137-144. PMID 11263872 DOI: 10.1021/Ar000108J |
0.556 |
|
| 2001 |
Spiro TG, Zgierski MZ, Kozlowski PM. Stereoelectronic factors in CO, NO and O2 binding to heme from vibrational spectroscopy and DFT analysis Coordination Chemistry Reviews. 219: 923-936. DOI: 10.1016/S0010-8545(01)00384-8 |
0.619 |
|
| 2001 |
Jarzcki AA, Spiro TG. Ab initio computation of the UV resonance Raman intensity pattern of aqueous imidazole Journal of Raman Spectroscopy. 32: 599-605. DOI: 10.1002/Jrs.730 |
0.409 |
|
| 2001 |
Kozlowski PM, Vogel KM, Zgierski MZ, Spiro TG. Steric contributions to CO binding in heme proteins: A density functional analysis of FeCO vibrations and deformability Journal of Porphyrins and Phthalocyanines. 5: 312-322. DOI: 10.1002/Jpp.318 |
0.595 |
|
| 2000 |
Eads DD, Moser C, Blackwood ME, Lin CY, Dutton L, Spiro TG. Selective enhancement of resonance Raman spectra of separate bacteriopheophytins in Rb. sphaeroides reaction centers Biopolymers - Biospectroscopy Section. 57: 64-76. PMID 10766957 DOI: 10.1002/(Sici)1097-0282(2000)57:2<64::Aid-Bip3>3.0.Co;2-A |
0.402 |
|
| 2000 |
Reynolds MF, Parks RB, Burstyn JN, Shelver D, Thorsteinsson MV, Kerby RL, Roberts GP, Vogel KM, Spiro TG. Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme. Biochemistry. 39: 388-96. PMID 10631000 DOI: 10.1021/Bi991378G |
0.391 |
|
| 2000 |
Zhao X, Chen R, Deng Q, Mabrouk PA, Spiro TG. UV resonance Raman probe of heme-bound imidazole established by 15N-labeling of hemoglobin Israel Journal of Chemistry. 40: 15-20. DOI: 10.1560/W4C5-891F-Bvrp-Xhul |
0.697 |
|
| 2000 |
Wang D, Zhao X, Spiro TG. Chain Selectivity of Tyrosine Contributions to Hemoglobin Static and Time-Resolved UVRR Spectra in 13C Isotopic Hybrids Journal of Physical Chemistry A. 104: 4149-4154. DOI: 10.1021/Jp992423X |
0.395 |
|
| 2000 |
Kozlowski PM, Spiro TG, Zgierski MZ. DFT study of structure and vibrations in low-lying spin states of five-coordinated deoxyheme model Journal of Physical Chemistry B. 104: 10659-10666. DOI: 10.1021/Jp001463U |
0.494 |
|
| 2000 |
Rush TS, Kozlowski PM, Piffat CA, Rumble R, Zgierski MZ, Spiro TG. Computational Modeling of Metalloporphyrin Structure and Vibrational Spectra: Porphyrin Ruffling in NiTPP Journal of Physical Chemistry B. 104: 5020-5034. DOI: 10.1021/Jp000266S |
0.649 |
|
| 2000 |
Wang D, Zhao X, Vargek M, Spiro TG. Metal-bound histidine modes in UV resonance Raman spectra of Cu, Zn superoxide dismutase Journal of the American Chemical Society. 122: 2193-2199. DOI: 10.1021/Ja992410X |
0.377 |
|
| 2000 |
Vogel KM, Kozlowski PM, Zgierski MZ, Spiro TG. Role of the axial ligand in heme-CO backbonding; DFT analysis of vibrational data Inorganica Chimica Acta. 297: 11-17. DOI: 10.1016/S0020-1693(99)00253-4 |
0.592 |
|
| 2000 |
Zhao X, Balakrishnan G, Moore EG, Spiro TG. Kinetics of hemoglobin allostery from time-resolved UV resonance Raman spectroscopy: Effect of a chemical cross-link Journal of Raman Spectroscopy. 31: 349-352. DOI: 10.1002/(Sici)1097-4555(200004)31:4<349::Aid-Jrs548>3.0.Co;2-6 |
0.39 |
|
| 1999 |
Fleissner G, Kozlowski PM, Vargek M, Bryson JW, O'Halloran TV, Spiro TG. UVRR Spectroscopy and Vibrational Analysis of Mercury Thiolate Compounds Resembling d(10) Metal Binding Sites in Proteins. Inorganic Chemistry. 38: 3523-3528. PMID 11671099 DOI: 10.1021/Ic9810384 |
0.638 |
|
| 1999 |
Vogel KM, Hu S, Spiro TG, Dierks EA, Yu AE, Burstyn JN. Variable forms of soluble guanylyl cyclase: protein-ligand interactions and the issue of activation by carbon monoxide. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 4: 804-13. PMID 10631613 DOI: 10.1007/S007750050354 |
0.388 |
|
| 1999 |
Dick LA, Heibel G, Moore EG, Spiro TG. UV resonance Raman spectra reveal a structural basis for diminished proton and CO2 binding to alpha,alpha-cross-linked hemoglobin. Biochemistry. 38: 6406-10. PMID 10350458 DOI: 10.1021/Bi981760D |
0.316 |
|
| 1999 |
Suen W, Spiro TG, Sowers LC, Fresco JR. Identification by UV resonance Raman spectroscopy of an imino tautomer of 5-hydroxy-2'-deoxycytidine, a powerful base analog transition mutagen with a much higher unfavored tautomer frequency than that of the natural residue 2'-deoxycytidine. Proceedings of the National Academy of Sciences of the United States of America. 96: 4500-5. PMID 10200291 DOI: 10.1073/Pnas.96.8.4500 |
0.424 |
|
| 1999 |
Hu X, Rodgers KR, Mukerji I, Spiro TG. New light on allostery: dynamic resonance Raman spectroscopy of hemoglobin kempsey. Biochemistry. 38: 3462-7. PMID 10090732 DOI: 10.1021/Bi982513C |
0.634 |
|
| 1999 |
Dong S, Ybe JA, Hecht MH, Spiro TG. H-bonding maintains the active site of type 1 copper proteins: site-directed mutagenesis of Asn38 in poplar plastocyanin. Biochemistry. 38: 3379-85. PMID 10079082 DOI: 10.1021/Bi981999U |
0.312 |
|
| 1999 |
Vogel KM, Spiro TG, Shelver D, Thorsteinsson MV, Roberts GP. Resonance Raman evidence for a novel charge relay activation mechanism of the CO-dependent heme protein transcription factor CooA. Biochemistry. 38: 2679-87. PMID 10052938 DOI: 10.1021/Bi982375R |
0.396 |
|
| 1999 |
Zhao X, Chen R, Tengroth C, Spiro TG. Solid-state tunable kHz ultraviolet laser for Raman applications Applied Spectroscopy. 53: 1200-1205. DOI: 10.1366/0003702991945669 |
0.63 |
|
| 1999 |
Rush TS, Kumble R, Spiro TG. Modeling the transient changes in the Soret-resonant Raman intensities of hemoglobin during the R → T transition Laser Chemistry. 19: 229-231. DOI: 10.1155/1999/70916 |
0.46 |
|
| 1999 |
Kozlowski PM, Rush TS, Jarzecki AA, Zgierski MZ, Chase B, Piffat C, Ye BH, Li XY, Pulay P, Spiro TG. DFT-SQM Force Field for Nickel Porphine: Intrinsic Ruffling Journal of Physical Chemistry A. 103: 1347-1356. DOI: 10.1021/Jp9819700 |
0.62 |
|
| 1999 |
Kozlowski PM, Rush TS, Jarzecki AA, Zgierski MZ, Chase B, Piffat C, Ye B, Li X, Pulay P, Spiro TG. DFT-SQM Force Field for Nickel Porphine: Intrinsic Ruffling The Journal of Physical Chemistry A. 103: 1357-1366. DOI: 10.1021/jp9819700 |
0.425 |
|
| 1999 |
Wang D, Zhao X, Shen TJ, Ho C, Spiro TG. Role of interhelical H-bonds (Wα14-Tα67 and Wβ15-Sβ72) in the hemoglobin allosteric reaction path evaluated by UV resonance Raman spectroscopy of site-mutants Journal of the American Chemical Society. 121: 11197-11203. DOI: 10.1021/Ja992228W |
0.419 |
|
| 1999 |
Vogel KM, Kozlowski PM, Zgierski MZ, Spiro TG. Determinants of the FeXo (X = C, N, O) vibrational frequencies in heme adducts from experiment and density functional theory Journal of the American Chemical Society. 121: 9915-9921. DOI: 10.1021/Ja990042R |
0.625 |
|
| 1999 |
Dong S, Padmakumar R, Banerjee R, Spiro TG. Co-C bond activation in B12-dependent enzymes: Cryogenic resonance Raman studies of methylmalonyl-coenzyme a mutase Journal of the American Chemical Society. 121: 7063-7070. DOI: 10.1021/Ja982753F |
0.399 |
|
| 1999 |
Fleissner G, Kozlowski PM, Vargek M, Bryson JW, O'Halloran TV, Spiro TG. UVRR spectroscopy and vibrational analysis of mercury thiolate compounds resembling d10 metal binding sites in proteins Inorganic Chemistry. 38: 3523-3528. DOI: 10.1021/ic9810384 |
0.509 |
|
| 1999 |
Vargek M, Zhao X, Lai Z, McLendon GL, Spiro TG. Monitoring cysteine and histidine ligands in zinc-finger peptides via ultraviolet resonance Raman spectroscopy Inorganic Chemistry. 38: 1372-1373. DOI: 10.1021/Ic980871Y |
0.367 |
|
| 1999 |
Wang D, Shin JY, Cheney MA, Sposito G, Spiro TG. Manganese dioxide as a catalyst for oxygen-independent atrazine dealkylation Environmental Science and Technology. 33: 3160-3165. DOI: 10.1021/Es990419T |
0.312 |
|
| 1999 |
Zhao X, Tengroth C, Chen R, Simpson WR, Spiro TG. Time-resolved Raman spectroscopy with a tunable ultraviolet kilohertz nanosecond laser Journal of Raman Spectroscopy. 30: 773-776. DOI: 10.1002/(Sici)1097-4555(199909)30:9<773::Aid-Jrs448>3.0.Co;2-R |
0.62 |
|
| 1999 |
Kozlowski PM, Rush TS, Jarzecki AA, Zgierski MZ, Chase B, Piffat C, Ye BH, Li XY, Pulay P, Spiro TG. DFT-SQM Force Field for Nickel Porphine: Intrinsic Ruffling Journal of Physical Chemistry A. 103: 1347-1356. |
0.425 |
|
| 1998 |
Zhao X, Wang D, Spiro TG. Detection of Metal-Bound Histidine in Ultraviolet Resonance Raman Spectra: Superoxide Dismutase. Inorganic Chemistry. 37: 5414-5415. PMID 11670681 DOI: 10.1021/Ic980705Q |
0.418 |
|
| 1998 |
Wang D, Spiro TG. Structure changes in hemoglobin upon deletion of C-terminal residues, monitored by resonance Raman spectroscopy. Biochemistry. 37: 9940-51. PMID 9665699 DOI: 10.1021/Bi980295H |
0.411 |
|
| 1998 |
Hu X, Dick LA, Spiro TG. Fourier transform infrared evidence against Asp beta 99 protonation in hemoglobin: nature of the Tyr alpha 42-Asp beta 99 quaternary H-bond. Biochemistry. 37: 9445-8. PMID 9649327 DOI: 10.1021/Bi9805644 |
0.322 |
|
| 1998 |
Blackwood ME, Rush TS, Romesberg F, Schultz PG, Spiro TG. Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions. Biochemistry. 37: 779-82. PMID 9457047 DOI: 10.1021/Bi972616F |
0.323 |
|
| 1998 |
Kumble R, Rush TS, Blackwood ME, Kozlowski PM, Spiro TG. Simulation of non-condon enhancement and interference effects in the resonance raman intensities of metalloporphyrins Journal of Physical Chemistry B. 102: 7280-7286. DOI: 10.1021/Jp9811225 |
0.634 |
|
| 1998 |
Kozlowski PM, Spiro TG, Bérces A, Zgierski MZ. Low-lying spin states of iron(II) porphine Journal of Physical Chemistry B. 102: 2603-2608. DOI: 10.1021/Jp973346D |
0.546 |
|
| 1998 |
Mabrouk PA, Spiro TG. New insights into horseradish peroxidase function in benzene from resonance Raman spectroscopy Journal of the American Chemical Society. 120: 10303-10309. DOI: 10.1021/Ja981711O |
0.436 |
|
| 1998 |
Dong S, Padmakumar R, Maiti N, Banerjee R, Spiro TG. Resonance raman spectra show that coenzyme B12 binding to methylmalonyl-coenzyme a mutase changes the corrin ring conformation but leaves the Co-C bond essentially unaffected [4] Journal of the American Chemical Society. 120: 9947-9948. DOI: 10.1021/Ja981584W |
0.405 |
|
| 1998 |
Dong S, Spiro TG. Ground- and excited-state mapping of plastocyanin from resonance Raman spectra of isotope-labeled proteins Journal of the American Chemical Society. 120: 10434-10440. DOI: 10.1021/Ja974377P |
0.433 |
|
| 1998 |
Zhao X, Wang D, Spiro TG. A UV resonance Raman monitor of histidine protonation in proteins: Bohr protons in hemoglobin [1] Journal of the American Chemical Society. 120: 8517-8518. DOI: 10.1021/Ja974040N |
0.401 |
|
| 1998 |
Spiro TG, KozlowsKi PM. Discordant results on FeCO deformability in heme proteins reconciled by density functional theory Journal of the American Chemical Society. 120: 4524-4525. DOI: 10.1021/Ja9732946 |
0.497 |
|
| 1998 |
Qiu D, Dasgupta S, Kozlowski PM, Goddard WA, Spiro TG. Chromophore-in-protein modeling of the structures and resonance Raman spectra for type 1 copper proteins Journal of the American Chemical Society. 120: 12791-12797. DOI: 10.1021/Ja964472I |
0.781 |
|
| 1998 |
Dong S, Padmakumar R, Banerjee R, Spiro TG. Co-C force constants from resonance Raman spectra of alkylcobalamins: Insensitivity to dimethylbenzylimidazole coordination Inorganica Chimica Acta. 270: 392-398. DOI: 10.1016/S0020-1693(97)05994-X |
0.395 |
|
| 1998 |
Smulevich G, Hu S, Rodgers KR, Goodin DB, Smith KM, Spiro TG. Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes Biospectroscopy. 2: 365-376. DOI: 10.1002/(SICI)1520-6343(1996)2:6<365::AID-BSPY3>3.0.CO;2-2 |
0.633 |
|
| 1998 |
Spiro TG, Kozlowski PM, Zgierski MZ. New developments in the calculation of metalloporphyrin Raman spectra via density functional theory Journal of Raman Spectroscopy. 29: 869-879. DOI: 10.1002/(Sici)1097-4555(199810/11)29:10/11<869::Aid-Jrs331>3.0.Co;2-T |
0.636 |
|
| 1998 |
Zhao X, Spiro TG. Ultraviolet Resonance Raman Spectroscopy of Hemoglobin with 200 and 212 nm Excitation: H-Bonds of Tyrosines and Prolines Journal of Raman Spectroscopy. 29: 49-55. DOI: 10.1002/(Sici)1097-4555(199801)29:1<49::Aid-Jrs216>3.0.Co;2-S |
0.43 |
|
| 1997 |
Sibilia SA, Hu S, Piffat C, Melamed D, Spiro TG. Metal Dependence of the Highest Occupied Molecular Orbital in Sterically Hindered Octaethyltetraphenylporphyrins. Inorganic Chemistry. 36: 1013-1019. PMID 11669663 DOI: 10.1021/Ic960774+ |
0.417 |
|
| 1997 |
Hu X, Spiro TG. Tyrosine and tryptophan structure markers in hemoglobin ultraviolet resonance Raman spectra: mode assignments via subunit-specific isotope labeling of recombinant protein. Biochemistry. 36: 15701-12. PMID 9398299 DOI: 10.1021/Bi971136L |
0.389 |
|
| 1997 |
Chan SS, Austin RH, Mukerji I, Spiro TG. Temperature-dependent ultraviolet resonance Raman spectroscopy of the premelting state of dA.dT DNA. Biophysical Journal. 72: 1512-20. PMID 9083657 DOI: 10.1016/S0006-3495(97)78799-X |
0.372 |
|
| 1997 |
Spiro TG. Resonance Raman Results: Retraction Science. 278: 17.9-20. DOI: 10.1126/Science.278.5335.17-I |
0.312 |
|
| 1997 |
Blackwood ME, Spiro TG. Resonance raman spectroscopic characterization of the π-anion and π-cation radicals of zinc(II) octaethylchlorin Journal of Physical Chemistry B. 101: 8363-8368. DOI: 10.1021/Jp971351B |
0.468 |
|
| 1997 |
Lin CY, Blackwood ME, Kumble R, Hu S, Spiro TG. Structural changes for π-radicals of free-base tetraphenylbacteriochlorin: A model for the electron donor and acceptor in bacterial reaction centers Journal of Physical Chemistry B. 101: 2372-2380. DOI: 10.1021/Jp963923I |
0.398 |
|
| 1997 |
Lin CY, Spiro TG. Resonance Raman, infrared, and normal coordinate analysis of free-base tetraphenylbacteriochlorin: A model for bacteriopheophytins Journal of Physical Chemistry B. 101: 472-482. DOI: 10.1021/Jp962479G |
0.421 |
|
| 1997 |
Blackwood ME, Lin CY, Cleary SR, McGlashen MM, Spiro TG. A resonance Raman spectroelectrochemical study of the Zn(II) tetraphenylchlorin anion Journal of Physical Chemistry A. 101: 255-258. DOI: 10.1021/Jp962081K |
0.458 |
|
| 1997 |
Qiu D, Kumar M, Ragsdale SW, Spiro TG. Raman and Infrared Spectroscopy of Cyanide-Inhibited CO Dehydrogenase/Acetyl-CoA Synthase fromClostridium thermoaceticum: Evidence for Bimetallic Enzymatic CO Oxidation [J.Am.Chem.Soc.1996,118, 10429−10435]. Journal of the American Chemical Society. 119: 11134-11135. DOI: 10.1021/Ja975422W |
0.34 |
|
| 1997 |
Qiu D, Kumar M, Ragsdale SW, Spiro TG. Freeze-Quench Resonance Raman Spectroscopic Evidence for an Fe−CO Adduct during Acetyl-CoA Synthesis and Ni Involvement in CO Oxidation by Carbon Monoxide Dehydrogenase fromClostridium thermoaceticumJ.Am.Chem.Soc.1995,117, 2653−2654 Journal of the American Chemical Society. 119: 11134-11135. DOI: 10.1021/Ja9754214 |
0.338 |
|
| 1997 |
Blackwood ME, Rush TS, Medlock A, Dailey HA, Spiro TG. Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding Journal of the American Chemical Society. 119: 12170-12174. DOI: 10.1021/Ja971619C |
0.459 |
|
| 1997 |
Sibilia SA, Czernuszewicz RS, Crossley MJ, Spiro TG. Orbital ordering in β-substituted porphyrins: Resonance raman spectra of the radical cations Inorganic Chemistry. 36: 6450-6453. DOI: 10.1021/Ic970562S |
0.423 |
|
| 1997 |
Vitols SE, Roman JS, Ryan DE, Blackwood ME, Spiro TG. Synthesis and Excited State Raman Spectroscopy of Sterically Crowded Ruthenium(II) Octaethyltetraphenylporphyrin Inorganic Chemistry. 36: 764-769. DOI: 10.1021/Ic960773H |
0.464 |
|
| 1997 |
Jayaraman V, Rodgers K, Mukerji I, Hu X, Spiro T. Metal coordination and protein dynamics: The allosteric reaction coordinate in hemoglobin Journal of Inorganic Biochemistry. 67: 79. DOI: 10.1016/S0162-0134(97)89959-X |
0.583 |
|
| 1997 |
Spiro TG, Kozlowski PM. Will the real FeCO please stand up? Journal of Biological Inorganic Chemistry. 2: 516-520. DOI: 10.1007/S007750050164 |
0.571 |
|
| 1996 |
Mukerji I, Shiber MC, Fresco JR, Spiro TG. A UV resonance Raman study of hairpin dimer helices of d(A-G)10 at neutral pH containing intercalated dA residues and alternating dG tetrads. Nucleic Acids Research. 24: 5013-20. PMID 9016674 DOI: 10.1093/Nar/24.24.5013 |
0.368 |
|
| 1996 |
Hu X, Frei H, Spiro TG. Nanosecond step-scan FTIR spectroscopy of hemoglobin: ligand recombination and protein conformational changes. Biochemistry. 35: 13001-5. PMID 8855934 DOI: 10.1021/Bi961522N |
0.395 |
|
| 1996 |
Blackwood ME, Kumble R, Spiro TG. Resonance Raman study of the T1 excited state of zinc(II) complexes of β-substituted chlorins Journal of Physical Chemistry. 100: 18037-18041. DOI: 10.1021/Jp961190W |
0.442 |
|
| 1996 |
Rush T, Kumble R, Mukherjee A, Blackwood ME, Spiro TG. Modeling the soret-resonant Raman intensities of metalloporphyrins and heme proteins. 1. Nickel porphine Journal of Physical Chemistry. 100: 12076-12085. DOI: 10.1021/Jp960660J |
0.459 |
|
| 1996 |
Vitols SE, Kumble R, Blackwood ME, Roman JS, Spiro TG. Charge transfer switching in photoexcited Ru(II) porphyrins: A time-resolved resonance raman and spectroelectrochemical study Journal of Physical Chemistry. 100: 4180-4187. DOI: 10.1021/Jp952618E |
0.432 |
|
| 1996 |
Pfennig BW, Wu Y, Kumble R, Spiro TG, Bocarsly AB. Time-dependent resonance Raman analysis of a trinuclear mixed valence coordination complex Journal of Physical Chemistry. 100: 5745-5750. DOI: 10.1021/Jp952108K |
0.422 |
|
| 1996 |
Vitols SE, Friesen DA, Williams DS, Melamed D, Spiro TG. Excited state dynamics of Rh(II) tetramesityl porphyrin monomer from nanosecond transient absorption and emission spectroscopy Journal of Physical Chemistry. 100: 207-213. DOI: 10.1021/Jp952003H |
0.354 |
|
| 1996 |
Hu S, Smith KM, Spiro TG. Assignment of protoheme Resonance Raman spectrum by heme labeling in myoglobin Journal of the American Chemical Society. 118: 12638-12646. DOI: 10.1021/Ja962239E |
0.474 |
|
| 1996 |
Lin CY, Hu S, Rush T, Spiro TG. Resonance Raman spectrum of distorted porphyrin radical cation reveals orbital mixing Journal of the American Chemical Society. 118: 9452-9453. DOI: 10.1021/Ja9621206 |
0.418 |
|
| 1996 |
Dong S, Padmakumar R, Banerjee R, Spiro TG. Resonance raman co-C stretching frequencies reflect bond strength changes in alkyl cobalamins, but are unaffected by trans ligand substitution Journal of the American Chemical Society. 118: 9182-9183. DOI: 10.1021/Ja962003A |
0.389 |
|
| 1996 |
Qiu D, Kumar M, Ragsdale SW, Spiro TG. Raman and infrared spectroscopy of cyanide-inhibited CO dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum: Evidence for bimetallic enzymatic CO oxidation Journal of the American Chemical Society. 118: 10429-10435. DOI: 10.1021/Ja960435F |
0.406 |
|
| 1996 |
Lin CY, Spiro TG. Structural Distortion of the Vanadyltetraphenylporphine Anion Radical Probed by Resonance Raman Spectroelectrochemistry Inorganic Chemistry. 35: 5237-5243. DOI: 10.1021/Ic960381A |
0.434 |
|
| 1996 |
Lin CY, McGlashen ML, Hu S, Shim YK, Smith KM, Spiro TG. Modeling the bonding changes in chlorophyll cation radicals: Resonance Raman spectroscopy of nickel (II) methyl pyropheophorbide a Inorganica Chimica Acta. 252: 179-184. DOI: 10.1016/S0020-1693(96)05312-1 |
0.4 |
|
| 1996 |
Jordan T, Mukerji I, Wang Y, Spiro TG. UV resonance Raman spectroscopy and hydrogen bonding of the proline peptide bond 1 Journal of Molecular Structure. 379: 51-64. DOI: 10.1016/0022-2860(95)09162-9 |
0.364 |
|
| 1996 |
Smulevich G, Hu S, Rodgers KR, Goodin DB, Smith KM, Spiro TG. Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance raman spectra of isotopically labeled hemes Biospectroscopy. 2: 365-376. DOI: 10.1002/(Sici)1520-6343(1996)2:6<365::Aid-Bspy3>3.0.Co;2-2 |
0.676 |
|
| 1996 |
Jayaraman V, Spiro TG. Structural evolution of the heme group during the allosteric transition in hemoglobin: Insights from resonance Raman spectra of isotopically labeled heme Biospectroscopy. 2: 311-316. DOI: 10.1002/(Sici)1520-6343(1996)2:5<311::Aid-Bspy4>3.0.Co;2-7 |
0.641 |
|
| 1995 |
Kilpatrick L, Rajagopalan KV, Hilton J, Bastian NR, Stiefel EI, Pilato RS, Spiro TG. Resonance Raman spectroscopic characterization of the molybdopterin active site of DMSO reductase. Biochemistry. 34: 3032-9. PMID 7893715 DOI: 10.1021/bi00009a034 |
0.333 |
|
| 1995 |
Austin JC, Fitzhugh A, Villafranca JE, Spiro TG. Stereoelectronic activation of methylenetetrahydrofolate by thymidylate synthase: Resonance Raman spectroscopic evidence Biochemistry. 34: 7678-7685. PMID 7779814 DOI: 10.1021/Bi00023A014 |
0.475 |
|
| 1995 |
Gregoriou VG, Jayaraman V, Hu X, Spiro TG. FT-IR difference spectroscopy of hemoglobins A and Kempsey: evidence that a key quaternary interaction induces protonation of Asp beta 99. Biochemistry. 34: 6876-82. PMID 7756319 DOI: 10.1021/Bi00020A035 |
0.579 |
|
| 1995 |
Spiro TG, Czernuszewicz RS. Resonance Raman spectroscopy of metalloproteins. Methods in Enzymology. 246: 416-60. PMID 7752933 DOI: 10.1016/0076-6879(95)46020-9 |
0.448 |
|
| 1995 |
Jayaraman V, Spiro TG. Structure of a third cooperativity state of hemoglobin: ultraviolet resonance Raman spectroscopy of cyanomethemoglobin ligation microstates. Biochemistry. 34: 4511-5. PMID 7718552 DOI: 10.1021/Bi00014A002 |
0.534 |
|
| 1995 |
Austin JC, Zhao Q, Jordan T, Talalay P, Mildvan AS, Spiro TG. Ultraviolet resonance Raman spectroscopy of delta 5-3-ketosteroid isomerase revisited: substrate polarization by active-site residues. Biochemistry. 34: 4441-7. PMID 7703258 DOI: 10.1021/Bi00013A037 |
0.383 |
|
| 1995 |
Jordan T, Eads JC, Spiro TG. Secondary and tertiary structure of the A-state of cytochrome c from resonance Raman spectroscopy. Protein Science : a Publication of the Protein Society. 4: 716-28. PMID 7613469 DOI: 10.1002/Pro.5560040411 |
0.464 |
|
| 1995 |
Mukerji I, Shiber MC, Spiro TG, Fresco JR. A UV resonance Raman study of d(A(+)-G)10, a single-stranded helix without stacked or paired bases. Biochemistry. 34: 14300-3. PMID 7578033 DOI: 10.1021/Bi00044A006 |
0.435 |
|
| 1995 |
Kumar M, Qiu D, Spiro TG, Ragsdale SW. A methylnickel intermediate in a bimetallic mechanism of acetyl-coenzyme A synthesis by anaerobic bacteria. Science (New York, N.Y.). 270: 628-30. PMID 7570019 DOI: 10.1126/Science.270.5236.628 |
0.303 |
|
| 1995 |
Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates. Science (New York, N.Y.). 269: 1843-8. PMID 7569921 DOI: 10.1126/Science.7569921 |
0.728 |
|
| 1995 |
Qiu D, Dong S, Ybe JA, Hecht MH, Spiro TG. Variations in the type I copper protein coordination group: Resonance Raman spectrum of 34S-, 65Cu-, and 15N-labeled plastocyanin Journal of the American Chemical Society. 117: 6443-6446. DOI: 10.1021/Ja00129A005 |
0.334 |
|
| 1995 |
Liu KE, Valentine AM, Qiu D, Edmondson DE, Appelman EH, Spiro TG, Lippard SJ. Characterization of a Diiron(III) Peroxide Intermediate in the Reaction Cycle of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath) Journal of the American Chemical Society. 117: 4997-4998. DOI: 10.1021/Ja00122A032 |
0.333 |
|
| 1995 |
Qiu D, Kumar M, Ragsdale SW, Spiro TG. Freeze-quench resonance Raman spectroscopic evidence for an Fe-CO adduct during acetyl-CoA synthesis and Ni involvement in CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum Journal of the American Chemical Society. 117: 2653-2654. DOI: 10.1021/Ja00114A032 |
0.34 |
|
| 1995 |
Hu S, Lin C, Blackwood ME, Mukherjee A, Spiro TG. Resonance Raman Structural Characterization of .beta.-Substituted Metalloporphyrins .pi.-Anion Radicals: Nature of the Jahn-Teller Effect The Journal of Physical Chemistry. 99: 9694-9701. DOI: 10.1021/J100024A009 |
0.351 |
|
| 1995 |
Vitols SE, Terashita SI, Blackwood ME, Kumble R, Ozaki Y, Spiro TG. Resonance Raman characterization of the triplet state of zinc tetraphenylchlorin Journal of Physical Chemistry. 99: 7246-7250. DOI: 10.1021/J100019A006 |
0.35 |
|
| 1995 |
Hu S, Spiro TG. Apparent depolarization dispersion in metalloporphyrin resonance Raman spectra can be an artifact of spectral crowding Journal of Physical Chemistry. 99: 7193-7194. DOI: 10.1021/J100018A062 |
0.436 |
|
| 1995 |
Kumble R, Loppnow GR, Hu S, Mukherjee A, Thompson MA, Spiro TG. Studies of the Vibrational and Electronic Structure of the S1 Excited States of .beta.-Substituted Porphyrins by Picosecond Time-Resolved Resonance Raman Spectroscopy The Journal of Physical Chemistry. 99: 5809-5816. DOI: 10.1021/J100016A014 |
0.691 |
|
| 1995 |
McGlashen ML, Eads DD, Spiro TG, Whittaker JW. Resonance Raman spectroscopy of galactose oxidase: A new interpretation based on model compound free radical spectra Journal of Physical Chemistry. 99: 4918-4922. DOI: 10.1021/J100014A008 |
0.394 |
|
| 1995 |
Mukherjee A, McGlashen ML, Spiro TG. Ultraviolet resonance Raman spectroscopy and general valence force field analysis of phenolate and phenoxyl radical Journal of Physical Chemistry. 99: 4912-4917. DOI: 10.1021/J100014A007 |
0.364 |
|
| 1995 |
Jordan T, Spiro TG. UV resonance Raman spectroscopy of cis--amides Journal of Raman Spectroscopy. 26: 867-876. DOI: 10.1002/Jrs.1250260838 |
0.377 |
|
| 1995 |
Hu S, Mukherjee A, Piffat C, Mak RSW, Li X, Spiro TG. Modeling the heme vibrational spectrum: Normal-mode analysis of nickel (II) etioporphyrin-I from resonance raman, ft-raman, and infrared spectra of multiple isotopomers Biospectroscopy. 1: 395-412. DOI: 10.1002/Bspy.350010605 |
0.434 |
|
| 1994 |
Austin JC, Rodgers KR, Spiro TG. Protein structure from ultraviolet resonance Raman spectroscopy. Methods in Enzymology. 226: 374-96. PMID 8277873 DOI: 10.1016/0076-6879(93)26017-4 |
0.692 |
|
| 1994 |
Rodgers KR, Spiro TG. Nanosecond dynamics of the R-->T transition in hemoglobin: ultraviolet Raman studies. Science (New York, N.Y.). 265: 1697-9. PMID 8085153 DOI: 10.1126/Science.8085153 |
0.596 |
|
| 1994 |
Mukerji I, Spiro TG. Modeling the hemoglobin switchpoint with cyanomet valency hybrids: Raman spectroscopic probes of tertiary and quaternary structure. Biochemistry. 33: 13132-9. PMID 7947719 DOI: 10.1021/Bi00248A024 |
0.406 |
|
| 1994 |
Sztainbuch IW, Soos ZG, Spiro TG. Herzberg-Teller coupling and configuration interaction in a metalloporphyrin model: 1,3,5,7-tetramethylcyclo-octatetraene dianion The Journal of Chemical Physics. 101: 4644-4648. DOI: 10.1063/1.467453 |
0.366 |
|
| 1994 |
Hu S, Vogel KM, Spiro TG. Deformability of Heme Protein CO Adducts: FT-IR Assignment of the FeCO Bending Mode Journal of the American Chemical Society. 116: 11187-11188. DOI: 10.1021/Ja00103A056 |
0.348 |
|
| 1994 |
Ling J, Nestor LP, Czernuszewicz RS, Spiro TG, Fraczkiewicz R, Sharma KD, Loehr TM, Sanders-Loehr J. Common Oxygen Binding Site in Hemocyanins from Arthropods and Mollusks. Evidence from Raman Spectroscopy and Normal Coordinate Analysis Journal of the American Chemical Society. 116: 7682-7691. DOI: 10.1021/Ja00096A027 |
0.325 |
|
| 1994 |
Czernuszewicz RS, Kilpatrick LK, Koch SA, Spiro TG. Resonance Raman Spectroscopy of Iron(III) Tetrathiolate Complexes: Implications for the Conformation and Force Field of Rubredoxin Journal of the American Chemical Society. 116: 7134-7141. DOI: 10.1021/Ja00095A017 |
0.392 |
|
| 1994 |
Yu AE, Hu S, Spiro TG, Burstyn JN. Resonance raman spectroscopy of soluble guanylyl cyclase reveals displacement of distal and proximal heme ligands by NO Journal of the American Chemical Society. 116: 4117-4118. DOI: 10.1021/Ja00088A073 |
0.42 |
|
| 1994 |
Kilpatrick LK, Kennedy MC, Beinert H, Czernuszewicz RS, Spiro TG, Qiu D. Cluster Structure and H-Bonding in Native, Substrate-Bound, and 3Fe Forms of Aconitase as Determined by Resonance Raman Spectroscopy Journal of the American Chemical Society. 116: 4053-4061. DOI: 10.1021/Ja00088A046 |
0.382 |
|
| 1994 |
Qiu D, Kilpatrick L, Kitajima N, Spiro TG. Modeling blue copper protein resonance Raman spectra with thiolate-CuII complexes of a sterically hindered tris(pyrazolyl)borate Journal of the American Chemical Society. 116: 2585-2590. DOI: 10.1021/Ja00085A044 |
0.426 |
|
| 1994 |
Ray GB, Li XY, Ibers JA, Sessler JL, Spiro TG. How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models Journal of the American Chemical Society. 116: 162-176. DOI: 10.1021/Ja00080A019 |
0.403 |
|
| 1994 |
Smulevich G, Bjerrum MJ, Gray HB, Spiro TG. Resonance raman spectra and the active site structure of semisynthetic Met80Cys horse heart cytochrome c Inorganic Chemistry. 33: 4629-4634. DOI: 10.1021/Ic00099A012 |
0.504 |
|
| 1994 |
Jordan T, Spiro TG. Enhancement of Cα hydrogen vibrations in the resonance Raman spectra of amides Journal of Raman Spectroscopy. 25: 537-543. DOI: 10.1002/Jrs.1250250715 |
0.479 |
|
| 1993 |
Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. R and T states of fluoromethemoglobin probed by ultraviolet resonance Raman spectroscopy. Biochemistry. 32: 4547-51. PMID 8485131 DOI: 10.1021/Bi00068A009 |
0.716 |
|
| 1993 |
Hu S, Morris IK, Singh JP, Smith KM, Spiro TG. Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes Journal of the American Chemical Society. 115: 12446-12458. DOI: 10.1021/Ja00079A028 |
0.445 |
|
| 1993 |
Hu S, Mukherjee A, Spiro TG. Synthesis, vibrational spectra, and normal mode analysis of nickel(II) 1,5-dihydroxy-1,5-dimethyloctaethylbacteriochlorin: a model for bacteriochlorophylls Journal of the American Chemical Society. 115: 12366-12377. DOI: 10.1021/Ja00079A018 |
0.411 |
|
| 1993 |
Hu S, Spiro TG. The origin of infrared marker bands of porphyrin .pi.-cation radicals: infrared assignments for cations of copper(II) complexes of octaethylporphine and tetraphenylporphine Journal of the American Chemical Society. 115: 12029-12034. DOI: 10.1021/Ja00078A047 |
0.387 |
|
| 1993 |
McGlashen ML, Blackwood ME, Spiro TG. Resonance Raman spectroelectrochemistry of the fullerene C60 radical anion Journal of the American Chemical Society. 115: 2074-2075. DOI: 10.1021/Ja00058A084 |
0.373 |
|
| 1993 |
Kumble R, Hu S, Loppnow GR, Vitols SE, Spiro TG. A time-resolved resonance Raman study of the T1 excited state of zinc(II) octaalkylporphyrins The Journal of Physical Chemistry. 97: 10521-10523. DOI: 10.1021/J100143A004 |
0.655 |
|
| 1993 |
Loppnow GR, Melamed D, Leheny AR, Hamilton AD, Spiro TG. Excited-state photophysics of donor-appended cobalt(II) porphyrins from picosecond transient absorption spectroscopy The Journal of Physical Chemistry. 97: 8969-8975. DOI: 10.1021/J100137A022 |
0.664 |
|
| 1993 |
Loppnow GR, Melamed D, Hamilton AD, Spiro TG. Charge transfer in covalently-linked porphyrin-donor complexes from picosecond transient absorption spectroscopy The Journal of Physical Chemistry. 97: 8957-8968. DOI: 10.1021/J100137A021 |
0.642 |
|
| 1993 |
Piffat C, Melamed D, Spiro TG. Ruffling effects on porphyrin vibrations: normal-mode analysis for nickel octaethyltetraphenylporphine from resonance Raman and IR spectra of isotopomers The Journal of Physical Chemistry. 97: 7441-7450. DOI: 10.1021/J100131A010 |
0.437 |
|
| 1993 |
Rodgers K, Mukerji I, Jayaraman V, Spiro T. Hemoglobin dynamics from transient raman spectroscopy Journal of Inorganic Biochemistry. 51: 215. DOI: 10.1016/0162-0134(93)85249-8 |
0.705 |
|
| 1993 |
Qiu D, Spiro TG. Resonance Raman study of vanadium bromoperoxidase and its model system Journal of Inorganic Biochemistry. 51: 128. DOI: 10.1016/0162-0134(93)85164-4 |
0.38 |
|
| 1992 |
Austin JC, Kuliopulos A, Mildvan AS, Spiro TG. Substrate polarization by residues in delta 5-3-ketosteroid isomerase probed by site-directed mutagenesis and UV resonance Raman spectroscopy. Protein Science : a Publication of the Protein Society. 1: 259-70. PMID 1339027 DOI: 10.1002/Pro.5560010208 |
0.433 |
|
| 1992 |
Rodgers KR, Su C, Subramaniam S, Spiro TG. Hemoglobin R.fwdarw.T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals Journal of the American Chemical Society. 114: 3697-3709. DOI: 10.1021/Ja00036A019 |
0.659 |
|
| 1992 |
Rodgers KR, Reed RA, Su YO, Spiro TG. Resonance Raman and magnetic resonance spectroscopic characterization of the Fe(I), Fe(II), Fe(III), and Fe(IV) oxidation states of Fe(2-TMPyP)n+(aq) Inorganic Chemistry. 31: 2688-2700. DOI: 10.1021/Ic00039A007 |
0.623 |
|
| 1992 |
Qiu D, Kilpatrick LT, Spiro TG, Kitajima N. Modelling copper protein resonance Raman study. Journal of Inorganic Biochemistry. 47: 56. DOI: 10.1016/0162-0134(92)84148-G |
0.373 |
|
| 1991 |
Smulevich G, Miller MA, Kraut J, Spiro TG. Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: Resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase Biochemistry. 30: 9546-9558. PMID 1654102 DOI: 10.1021/Bi00103A023 |
0.401 |
|
| 1991 |
Wang Y, Purrello R, Georgiou S, Spiro TG. UVRR spectroscopy of the peptide bond. 2. Carbonyl H-bond effects on the ground- and excited-state structures of N-methylacetamide Journal of the American Chemical Society. 113: 6368-6377. DOI: 10.1021/Ja00017A003 |
0.325 |
|
| 1991 |
Wang Y, Purrello R, Jordan T, Spiro TG. UVRR spectroscopy of the peptide bond. 1. Amide S, a nonhelical structure marker, is a C.alpha.H bending mode Journal of the American Chemical Society. 113: 6359-6368. DOI: 10.1021/Ja00017A002 |
0.312 |
|
| 1991 |
Reed RA, Purrello R, Prendergast K, Spiro TG. Resonance Raman characterization of the radical anion and triplet states of zinc tetraphenylporphine Journal of Physical Chemistry. 95: 9720-9727. DOI: 10.1021/J100177A024 |
0.387 |
|
| 1991 |
Melamed D, Sullivan EP, Prendergast K, Strauss SH, Spiro TG. Analysis of a siroheme model compound: Core-size dependence of Resonance Raman bands and the siroheme spin state in sulfite reductase Inorganic Chemistry. 30: 1308-1319. DOI: 10.1021/Ic00006A028 |
0.477 |
|
| 1991 |
Stiefel EJ, Pilato R, Eriksen K, Greaney M, Goswami S, Taylor E, Kilpatrick L, Spiro T, Rheingold A. Chemistry related to the structure, spectra and reactivity of molybdopterin (Mo-co) dependent enzymes Journal of Inorganic Biochemistry. 43: 574. DOI: 10.1016/0162-0134(91)84547-M |
0.329 |
|
| 1991 |
Vitols SE, Kumble R, Spiro TG. Time-resolved resonance Raman study of the radical anion of (tetraphenylporphinato)bis(pyridine) ruthenium(II). Journal of Inorganic Biochemistry. 43: 331. DOI: 10.1016/0162-0134(91)84318-4 |
0.393 |
|
| 1991 |
Molina M, Wang Y, Purrello R, Spiro TG. Dinucleotide binding to RNase probed with UV resonance Raman spectroscopy Journal of Raman Spectroscopy. 22: 205-209. DOI: 10.1002/Jrs.1250220403 |
0.458 |
|
| 1990 |
Smulevich G, Miller MA, Gosztola D, Spiro TG. Photodissociable endogenous ligand in alkaline-reduced cytochrome c peroxidase implicates distal protein tension. Biochemistry. 28: 9905-8. PMID 2559773 DOI: 10.1021/Bi00452A004 |
0.596 |
|
| 1990 |
Smulevich G, Wang Y, Mauro JM, Wang JM, Fishel LA, Kraut J, Spiro TG. Single-crystal resonance Raman spectroscopy of site-directed mutants of cytochrome c peroxidase. Biochemistry. 29: 7174-80. PMID 2169874 DOI: 10.1021/Bi00483A004 |
0.318 |
|
| 1990 |
Spiro TG, Smulevich G, Su C. Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome c peroxidase and hemoglobin. Biochemistry. 29: 4497-508. PMID 2164841 DOI: 10.1021/Bi00471A001 |
0.403 |
|
| 1990 |
Ray GB, Copeland RA, Lee CP, Spiro TG. Resonance Raman evidence for low-spin Fe2+ heme a3 in energized cytochrome c oxidase: implications for the inhibition of O2 reduction. Biochemistry. 29: 3208-13. PMID 2159329 DOI: 10.1021/Bi00465A009 |
0.365 |
|
| 1990 |
Smulevich G, Wang Y, Edwards SL, Poulos TL, English AM, Spiro TG. Resonance Raman spectroscopy of cytochrome c peroxidase single crystals on a variable-temperature microscope stage. Biochemistry. 29: 2586-92. PMID 2159325 DOI: 10.1021/Bi00462A022 |
0.403 |
|
| 1990 |
Gruber S, Kilpatrick L, Bastian NR, Rajagopalan KV, Spiro TG. Dithiolene coordination in the molybdopterin cofactor of DMSO reductase: in situ evidence from resonance Raman spectroscopy Journal of the American Chemical Society. 112: 8179-8180. DOI: 10.1021/Ja00178A059 |
0.44 |
|
| 1990 |
Hildebrandt P, Tsuboi M, Spiro TG. Ultraviolet resonance Raman spectroscopy of formamide: evidence for n-.pi.* interferences and intermolecular vibronic coupling The Journal of Physical Chemistry. 94: 2274-2279. DOI: 10.1021/J100369A015 |
0.589 |
|
| 1990 |
Li XY, Czernuszewicz RS, Kincaid JR, Stein P, Spiro TG. Consistent porphyrin force field. 2. Nickel octaethylporphyrin skeletal and substituent mode assignments from nitrogen-15, meso-d4, and methylene-d16 Raman and infrared isotope shifts The Journal of Physical Chemistry. 94: 47-61. DOI: 10.1021/J100364A008 |
0.427 |
|
| 1990 |
Li XY, Czernuszewicz RS, Kincaid JR, Su YO, Spiro TG. Consistent porphyrin force field. 1. Normal-mode analysis for nickel porphine and nickel tetraphenylporphine from resonance Raman and infrared spectra and isotope shifts The Journal of Physical Chemistry. 94: 31-47. DOI: 10.1021/J100364A007 |
0.375 |
|
| 1990 |
Subramanian P, Burgmayer S, Richards S, Szalai V, Spiro TG. Resonance Raman signatures of oxomolybdenum thiolate and dithiolene models of molybdenum proteins Inorganic Chemistry. 29: 3849-3853. DOI: 10.1021/Ic00344A039 |
0.377 |
|
| 1990 |
Reed RA, Rodgers KR, Kushmeider K, Spiro TG, Su YO. Iron-hydroxide stretching resonance Raman bands of a water-soluble sterically hindered porphyrin Inorganic Chemistry. 29: 2881-2883. DOI: 10.1021/Ic00341A003 |
0.641 |
|
| 1990 |
Macor KA, Czernuszewicz RS, Spiro TG. Influence of porphyrin radical type on vanadium-oxygen double bond strength in vanadyl porphyrin cation radicals: implications for heme protein intermediates Inorganic Chemistry. 29: 1996-2000. DOI: 10.1021/Ic00335A044 |
0.32 |
|
| 1990 |
Spiro TG, Czernuszewicz RS, Li X. Metalloporphyrin structure and dynamics from resonance raman spectroscopy Coordination Chemistry Reviews. 100: 541-571. DOI: 10.1016/0010-8545(90)85019-O |
0.393 |
|
| 1990 |
Su C, Wang Y, Spiro TG. Saturation effects on ultraviolet resonance Raman intensities: Excimer/YAG laser comparison and aromatic amino acid cross-sections Journal of Raman Spectroscopy. 21: 435-440. DOI: 10.1002/Jrs.1250210709 |
0.369 |
|
| 1990 |
Grygon CA, Spiro TG. Uv resonance Raman spectroscopy of nucleic acid duplexes containing A-U and A-T base pairs Biopolymers. 29: 707-715. DOI: 10.1002/Bip.360290405 |
0.396 |
|
| 1989 |
Grygon CA, Spiro TG. Ultraviolet resonance Raman spectroscopy of distamycin complexes with poly(dA)-poly(dT) and poly(dA-dT): role of H-bonding. Biochemistry. 28: 4397-402. PMID 2765491 DOI: 10.1021/Bi00436A041 |
0.465 |
|
| 1989 |
Han SH, Madden JF, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. Biochemistry. 28: 5477-85. PMID 2673348 DOI: 10.1021/Bi00439A024 |
0.42 |
|
| 1989 |
Madden JF, Han SH, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. Biochemistry. 28: 5471-7. PMID 2673347 DOI: 10.1021/Bi00439A023 |
0.439 |
|
| 1989 |
Han SH, Madden JF, Thompson RG, Strauss SH, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry. 28: 5461-71. PMID 2673346 DOI: 10.1021/Bi00439A022 |
0.421 |
|
| 1989 |
Liu GY, Grygon CA, Spiro TG. Ionic strength dependence of cytochrome c structure and Trp-59 H/D exchange from ultraviolet resonance Raman spectroscopy. Biochemistry. 28: 5046-50. PMID 2548599 DOI: 10.1021/Bi00438A022 |
0.425 |
|
| 1989 |
Ramsden J, Spiro TG. Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin. Biochemistry. 28: 3125-8. PMID 2545246 DOI: 10.1021/Bi00434A001 |
0.421 |
|
| 1989 |
Wang Y, Purrello R, Spiro TG. UV photoisomerization of N-methylacetamide and resonance Raman enhancement of a new conformation-sensitive amide mode Journal of the American Chemical Society. 111: 8274-8276. DOI: 10.1021/Ja00203A037 |
0.388 |
|
| 1989 |
Czernuszewicz RS, Li XY, Spiro TG. Nickel octaethylporphyrin ruffling dynamics from resonance Raman spectroscopy Journal of the American Chemical Society. 111: 7024-7031. DOI: 10.1021/Ja00200A019 |
0.397 |
|
| 1989 |
Li XY, Czernuszewicz RS, Kincaid JR, Spiro TG. Consistent porphyrin force field. 3. Out-of-plane modes in the resonance Raman spectra of planar and ruffled nickel octaethylporphyrin Journal of the American Chemical Society. 111: 7012-7023. DOI: 10.1021/Ja00200A018 |
0.408 |
|
| 1989 |
Fodor SPA, Copeland RA, Grygon CA, Spiro TG. Deep-ultraviolet Raman excitation profiles and vibronic scattering mechanisms of phenylalanine, tyrosine, and tryptophan Journal of the American Chemical Society. 111: 5509-5518. DOI: 10.1021/Ja00197A001 |
0.346 |
|
| 1989 |
Czernuszewicz RS, Macor KA, Li XY, Kincaid JR, Spiro TG. Resonance Raman spectroscopy reveals a1u vs. a2u character and pseudo-Jahn-Teller distortion in radical cations of nickel(II), copper(II), and chloroiron(III) octaethyl- and tetraphenylporphyrins Journal of the American Chemical Society. 111: 3860-3869. DOI: 10.1021/Ja00193A017 |
0.352 |
|
| 1989 |
Han S, Czernuszewicz RS, Kimura T, Adams MWW, Spiro TG. Fe2S2 protein resonance Raman spectra revisited: structural variations among adrenodoxin, ferredoxin, and red paramagnetic protein Journal of the American Chemical Society. 111: 3505-3511. DOI: 10.1021/Ja00192A003 |
0.406 |
|
| 1989 |
Han S, Czernuszewicz RS, Spiro TG. Vibrational spectra and normal mode analysis for [2Fe-2S] protein analogs using sulfur-34, iron-54 and deuterium substitution: coupling of iron-sulfur stretching and sulfur-carbon-carbon bending modes Journal of the American Chemical Society. 111: 3496-3504. DOI: 10.1021/Ja00192A002 |
0.356 |
|
| 1989 |
Su C, Park YD, Liu GY, Spiro TG. Hemoglobin quaternary structure change monitored directly by transient UV resonance Raman spectroscopy Journal of the American Chemical Society. 111: 3457-3459. DOI: 10.1021/Ja00191A068 |
0.409 |
|
| 1989 |
Anzenbacher P, Evangelista-Kirkup R, Schenkman J, Spiro TG. Influence of thiolate ligation on the heme electronic structure in microsomal cytochrome P-450 and model compounds: resonance Raman spectroscopic evidence Inorganic Chemistry. 28: 4491-4495. DOI: 10.1021/Ic00324A013 |
0.342 |
|
| 1989 |
Spiro TG. Biological applications of raman spectroscopy. Vol. 3: resonance raman spectra of heme and metalloproteins Analytica Chimica Acta. 218: 356. DOI: 10.1016/S0003-2670(00)80321-9 |
0.339 |
|
| 1989 |
Hildebrandt P, Czernuszewicz RS, Grygon CA, Spiro TG. Ultraviolet resonance Raman enhancement of the carboxylate and guanidinium groups in amino acids Journal of Raman Spectroscopy. 20: 645-650. DOI: 10.1002/Jrs.1250201003 |
0.63 |
|
| 1988 |
Hildebrandt PG, Copeland RA, Spiro TG, Otlewski J, Laskowski M, Prendergast FG. Tyrosine hydrogen-bonding and environmental effects in proteins probed by ultraviolet resonance Raman spectroscopy. Biochemistry. 27: 5426-33. PMID 3179264 DOI: 10.1021/Bi00415A007 |
0.398 |
|
| 1988 |
Smulevich G, Mauro JM, Fishel LA, English AM, Kraut J, Spiro TG. Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts. Biochemistry. 27: 5486-92. PMID 2846040 |
0.334 |
|
| 1988 |
Smulevich G, Mauro JM, Fishel LA, English AM, Kraut J, Spiro TG. Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy. Biochemistry. 27: 5477-85. PMID 2846039 |
0.332 |
|
| 1988 |
Su YO, Czernuszewicz RS, Miller LA, Spiro TG. Effects of solvents, axial ligation, and radical cation formation on the V:O stretching Raman frequency in vanadyl porphyrins. Implications for peroxidase intermediates Journal of the American Chemical Society. 110: 4150-4157. DOI: 10.1021/Ja00221A009 |
0.354 |
|
| 1988 |
Hildebrandt P, Spiro TG. Surface-enhanced resonance Raman spectroscopy of copper chlorophyllin on silver and gold colloids The Journal of Physical Chemistry. 92: 3355-3360. DOI: 10.1021/J100323A010 |
0.612 |
|
| 1988 |
Spiro TG, Grygon CA. Applications of ultraviolet resonance raman spectroscopy to proteins Journal of Molecular Structure. 173: 79-90. DOI: 10.1016/0022-2860(88)80044-9 |
0.441 |
|
| 1988 |
Su Y, Kim D, Spiro TG. Isoporphyrin formation upon electrochemical oxidation of zinc tetrakis(4-sulfonato-phenyl)porphine in aqueous solution Journal of Electroanalytical Chemistry and Interfacial Electrochemistry. 246: 363-371. DOI: 10.1016/0022-0728(88)80172-4 |
0.31 |
|
| 1988 |
Perno JR, Park YD, Reedijk J, Spiro TG. UV resonance Raman study of platinum binding to guanine in mono- and di-nucleotides Journal of Raman Spectroscopy. 19: 203-212. DOI: 10.1002/Jrs.1250190311 |
0.371 |
|
| 1988 |
CZERNUSZEWICZ RS, SU YO, STERN MK, MACOR KA, KIM D, GROVES JT, SPIRO TG. ChemInform Abstract: Oxomanganese(IV) Porphyrins Identified by Resonance Raman and IR Spectroscopy: Weak Bonds and the Stability of the Half-Filled t2g Subshell. Cheminform. 19. DOI: 10.1002/chin.198842281 |
0.311 |
|
| 1987 |
Dasgupta S, Spiro TG. Resonance Raman characterization of the 7-ns photoproduct of (carbonmonoxy)hemoglobin: implications for hemoglobin dynamics. Biochemistry. 25: 5941-8. PMID 3790496 DOI: 10.1021/Bi00368A016 |
0.724 |
|
| 1987 |
Copeland RA, Spiro TG. Secondary structure determination in proteins from deep (192-223-nm) ultraviolet Raman spectroscopy. Biochemistry. 26: 2134-9. PMID 3620443 DOI: 10.1021/Bi00382A011 |
0.403 |
|
| 1987 |
Czernuszewicz RS, Macor KA, Johnson MK, Gewirth A, Spiro TG. Vibrational mode structure and symmetry in proteins and analogs containing Fe4S4 clusters: resonance Raman evidence that HiPIP is tetrahedral while ferredoxin undergoes a D2d distortion Journal of the American Chemical Society. 109: 7178-7187. DOI: 10.1021/Ja00257A045 |
0.591 |
|
| 1987 |
Caswell DS, Spiro TG. Proline signals in ultraviolet resonance Raman spectra of proteins: cis-trans isomerism in polyproline and ribonuclease A Journal of the American Chemical Society. 109: 2796-2800. DOI: 10.1021/Ja00243A037 |
0.385 |
|
| 1987 |
Mitchell ML, Li XY, Kincaid JR, Spiro TG. Axial ligand and out-of-plane vibrations for bis(imidazolyl)heme: Raman and infrared iron-54, nitrogen-15, and deuterium isotope shifts and normal coordinate calculations The Journal of Physical Chemistry. 91: 4690-4696. DOI: 10.1021/J100302A013 |
0.415 |
|
| 1987 |
Parthasarathi N, Spiro TG. Axial ligation of manganese(III/II) heme complexes and manganese-substituted myoglobin and hemoglobin from resonance Raman spectroscopy Inorganic Chemistry. 26: 3792-3796. DOI: 10.1021/Ic00269A033 |
0.41 |
|
| 1987 |
Macor KA, Su YO, Miller LA, Spiro TG. Electrochemical and resonance Raman spectroscopic characterization of polyaniline and polyaniline-metalloporphyrin electrode films Inorganic Chemistry. 26: 2594-2598. DOI: 10.1021/Ic00263A009 |
0.307 |
|
| 1987 |
Parthasarathi N, Spiro TG. Bonding in nitrosyl adducts of manganese-substituted hemoglobin and myoglobin monitored by resonance Raman spectroscopy Inorganic Chemistry. 26: 2280-2282. DOI: 10.1021/Ic00261A023 |
0.43 |
|
| 1987 |
Czernuszewicz RS, Sheats JE, Spiro TG. Resonance Raman spectra and excitation profile for bis(acetato)bis(hydrotripyrazolylborato)oxodiiron, a hemerythrin analog Inorganic Chemistry. 26: 2063-2067. DOI: 10.1021/Ic00260A011 |
0.46 |
|
| 1987 |
Perno JR, Cwikel D, Spiro TG. Ultraviolet resonance Raman study of deoxyguanosine monophosphate and its complexes with cis-(NH3)Pt2+, Ni2+ and H+ Inorganic Chemistry. 26: 400-405. DOI: 10.1021/Ic00250A013 |
0.327 |
|
| 1987 |
PARTHASARATHI N, SPIRO TG. ChemInform Abstract: Bonding in Nitrosyl Adducts of Manganese-Substituted Hemoglobin and Myoglobin Monitored by Resonance Raman Spectroscopy Cheminform. 18. DOI: 10.1002/CHIN.198745065 |
0.322 |
|
| 1987 |
CZERNUSZEWICZ RS, SHEATS JE, SPIRO TG. ChemInform Abstract: Resonance Raman Spectra and Excitation Profile for (Fe2O(O2CCH3)2(HB(pz)3)2), a Hemerythrin Analogue Cheminform. 18. DOI: 10.1002/chin.198745048 |
0.35 |
|
| 1987 |
KIM D, SU YO, SPIRO TG. ChemInform Abstract: Back-Bonding in the Ruthenium Porphyrins (I) and (II) as Monitored by Resonance Raman Spectroscopy. Cheminform. 18. DOI: 10.1002/CHIN.198710049 |
0.305 |
|
| 1987 |
SORRELL TN, BOROVIK AS, CASWELL DS, GRYGON C, SPIRO TG. ChemInform Abstract: UV Absorption and Resonance Raman Spectra of Copper(I) Complexes Cheminform. 18. DOI: 10.1002/CHIN.198702046 |
0.318 |
|
| 1986 |
Evangelista-Kirkup R, Smulevich G, Spiro TG. Alternative carbon monoxide binding modes for horseradish peroxidase studied by resonance Raman spectroscopy. Biochemistry. 25: 4420-5. PMID 3756147 DOI: 10.1021/Bi00363A037 |
0.442 |
|
| 1986 |
Coppey M, Dasgupta S, Spiro TG. Resonance Raman spectroscopic evidence that carp deoxyhemoglobin remains in a T-like quaternary structure at high pH: implications for cooperativity. Biochemistry. 25: 1940-4. PMID 3707921 DOI: 10.1021/Bi00356A016 |
0.715 |
|
| 1986 |
Nestor L, Reinhammar B, Spiro TG. 63/65Cu and 1/2H2O isotope shifts in the low-temperature resonance Raman spectrum of fungal laccase. Biochimica Et Biophysica Acta. 869: 286-92. PMID 3511965 DOI: 10.1016/0167-4838(86)90068-3 |
0.401 |
|
| 1986 |
Caswell DS, Spiro TG. Tyrosine and tryptophan modification monitored by ultraviolet resonance Raman spectroscopy. Biochimica Et Biophysica Acta. 873: 73-8. PMID 3091073 DOI: 10.1016/0167-4838(86)90191-3 |
0.456 |
|
| 1986 |
Smulevich G, Evangelista-Kirkup R, English A, Spiro TG. Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states. Biochemistry. 25: 4426-30. PMID 3019391 DOI: 10.1021/Bi00363A038 |
0.421 |
|
| 1986 |
Smulevich G, Dasgupta S, English A, Spiro TG. Transient resonance Raman spectroscopy shows unrelaxed heme following CO photodissociation from cytochrome-c peroxidase. Biochimica Et Biophysica Acta. 873: 88-91. PMID 3017436 DOI: 10.1016/0167-4838(86)90193-7 |
0.731 |
|
| 1986 |
Copeland RA, Spiro TG. Resonance Raman evidence for an exchangeable protein hydrogen associated with the heme a group of cytochrome oxidase. Febs Letters. 197: 239-43. PMID 3005042 DOI: 10.1016/0014-5793(86)80334-9 |
0.43 |
|
| 1986 |
Copeland RA, Spiro TG. Ultraviolet resonance Raman spectra of cytochrome c conformational states. Biochemistry. 24: 4960-8. PMID 3000420 DOI: 10.1021/Bi00339A035 |
0.417 |
|
| 1986 |
Fitzhugh AL, Fodor S, Kaufman S, Spiro TG. Resonance Raman spectroscopic evidence for alternative structures in the native ternary complex formed with thymidylate synthase Journal of the American Chemical Society. 108: 7422-7424. DOI: 10.1021/Ja00283A055 |
0.393 |
|
| 1986 |
Caswell DS, Spiro TG. Ultraviolet resonance Raman spectroscopy of imidazole, histidine, and Cu(imidazole)42+: implications for protein studies Journal of the American Chemical Society. 108: 6470-6477. DOI: 10.1021/Ja00281A004 |
0.372 |
|
| 1986 |
Sorrell TN, Borovik AS, Caswell DS, Grygon C, Spiro TG. Ultraviolet absorption and resonance Raman spectra of copper(I) complexes Journal of the American Chemical Society. 108: 5636-5637. DOI: 10.1021/Ja00278A051 |
0.429 |
|
| 1986 |
Fodor SPA, Spiro TG. Ultraviolet resonance Raman spectroscopy of DNA with 200-266-nm laser excitation Journal of the American Chemical Society. 108: 3198-3205. DOI: 10.1021/Ja00272A006 |
0.37 |
|
| 1986 |
Kim D, Spiro TG. Laser-induced excited-state ligation changes for nickel tetraphenylporphine monitored by Raman spectroscopy Journal of the American Chemical Society. 108: 2099-2100. DOI: 10.1021/Ja00268A065 |
0.376 |
|
| 1986 |
Kim D, Terner J, Spiro TG. Excited triplet state resonance Raman spectra of magnesium, zinc, and palladium tetraphenylporphine Journal of the American Chemical Society. 108: 2097-2099. DOI: 10.1021/Ja00268A064 |
0.413 |
|
| 1986 |
Copeland RA, Spiro TG. Ultraviolet Raman hypochromism of the tropomyosin amide modes: a new method for estimating .alpha.-helical content in proteins Journal of the American Chemical Society. 108: 1281-1285. DOI: 10.1021/Ja00266A025 |
0.302 |
|
| 1986 |
Kim D, Miller LA, Rakhit G, Spiro TG. Resonance Raman spectra of metallooctaethylporphyrin cation radicals with alu and a2u orbital character The Journal of Physical Chemistry. 90: 3320-3325. DOI: 10.1021/J100406A005 |
0.38 |
|
| 1986 |
Copeland RA, Spiro TG. Ultraviolet resonance Raman spectroscopy of flavin mononucleotide and flavin-adenine dinucleotide The Journal of Physical Chemistry. 90: 6648-6654. DOI: 10.1021/J100283A011 |
0.435 |
|
| 1986 |
Kim D, Su YO, Spiro TG. Back-bonding in ruthenium porphyrins as monitored by resonance Raman spectroscopy Inorganic Chemistry. 25: 3993-3997. DOI: 10.1021/Ic00242A034 |
0.36 |
|
| 1986 |
Kim D, Su YO, Spiro TG. Resonance Raman frequencies and core size for low- and high-spin nickel porphyrins Inorganic Chemistry. 25: 3988-3993. DOI: 10.1021/Ic00242A033 |
0.39 |
|
| 1986 |
Kim D, Miller LA, Spiro TG. Intramolecular electron transfer in the one-electron oxidation product of (tetraphenylporphinato)nickel(II), as studied by resonance Raman spectroscopy Inorganic Chemistry. 25: 2468-2470. DOI: 10.1021/Ic00234A037 |
0.331 |
|
| 1986 |
Czernuszewicz RS, LeGall J, Moura I, Spiro TG. Resonance Raman spectra of rubredoxin: new assignments and vibrational coupling mechanism from iron-54/iron-56 isotope shifts and variable-wavelength excitation Inorganic Chemistry. 25: 696-700. DOI: 10.1021/Ic00225A022 |
0.419 |
|
| 1986 |
Smulevich G, Evangelista-Kirkup R, English A, Spiro T. Two CO binding modes for HRPCO and CCPCO: Raman evidence of CO pressure and pH dependence Journal of Molecular Structure. 141: 411-414. DOI: 10.1016/0022-2860(86)80358-1 |
0.398 |
|
| 1986 |
Fodor SPA, Rava RP, Copeland RA, Spiro TG. H2 Raman-shifted YAG laser ultraviolet Raman spectrometer operating at wavelengths down to 184 nm Journal of Raman Spectroscopy. 17: 471-475. DOI: 10.1002/Jrs.1250170609 |
0.394 |
|
| 1986 |
KIM D, TERNER J, SPIRO TG. ChemInform Abstract: Excited Triplet State Resonance Raman Spectra of Magnesium, Zinc, and Palladium Tetraphenylporphine. Chemischer Informationsdienst. 17. DOI: 10.1002/chin.198632046 |
0.33 |
|
| 1986 |
Feitelson J, Spiro TG. Bonding in zinc proto- and mesoporphyrin substituted myoglobin and model compounds studied by resonance Raman spectroscopy Inorganic Chemistry. 25: 861-865. DOI: 10.1002/Chin.198628042 |
0.387 |
|
| 1986 |
CZERNUSZEWICZ RS, LEGALL J, MOURA I, SPIRO TG. ChemInform Abstract: Resonance Raman Spectra of Rubredoxin: New Assignments and Vibrational Coupling Mechanism from 54Fe/56Fe Isotope Shifts and Variable-Wavelength Excitation. Chemischer Informationsdienst. 17. DOI: 10.1002/Chin.198628041 |
0.418 |
|
| 1985 |
Dasgupta S, Spiro TG, Johnson CK, Dalickas GA, Hochstrasser RM. Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct. Biochemistry. 24: 5295-7. PMID 4074696 DOI: 10.1021/Bi00341A003 |
0.743 |
|
| 1985 |
Fodor SP, Starr PA, Spiro TG. Raman spectroscopic elucidation of DNA backbone conformations for poly(dG-dT).poly(dA-dC) and poly(dA-dT).poly(dA-dT) in CsF solution. Biopolymers. 24: 1493-500. PMID 4041547 DOI: 10.1002/Bip.360240806 |
0.349 |
|
| 1985 |
Smulevich G, Spiro TG. Nanosecond transient resonance Raman spectra of the FeII-CO and FeIII-NO photolysis products of horseradish peroxidase. Biochimica Et Biophysica Acta. 830: 80-5. PMID 4016131 DOI: 10.1016/0167-4838(85)90134-7 |
0.458 |
|
| 1985 |
Rava RP, Spiro TG. Ultraviolet resonance Raman spectra of insulin and alpha-lactalbumin with 218- and 200-nm laser excitation. Biochemistry. 24: 1861-5. PMID 3893540 DOI: 10.1021/Bi00329A009 |
0.472 |
|
| 1985 |
Spiro TG. Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. Advances in Protein Chemistry. 37: 111-59. PMID 2998161 DOI: 10.1016/S0065-3233(08)60064-9 |
0.467 |
|
| 1985 |
Evangelista-Kirkup R, Crisanti M, Poulos TL, Spiro TG. Resonance Raman spectroscopy shows different temperature-dependent coordination equilibria for native horseradish and cytochrome c peroxidase Febs Letters. 190: 221-226. PMID 2995134 DOI: 10.1016/0014-5793(85)81288-6 |
0.382 |
|
| 1985 |
Copeland RA, Naqui A, Chance B, Spiro TG. Resonance Raman spectroscopy and enhanced photoreducibility for the 420 nm pulsed form of cytochrome oxidase. Febs Letters. 182: 375-9. PMID 2984043 DOI: 10.1016/0014-5793(85)80336-7 |
0.375 |
|
| 1985 |
Cartling B, Holtom GR, Spiro TG. Photoelectron generation and transfer to cytochrome c studied by nanosecond transient absorption spectroscopy The Journal of Chemical Physics. 83: 3894-3905. DOI: 10.1063/1.449101 |
0.304 |
|
| 1985 |
Copeland RA, Dasgupta S, Spiro TG. Ultraviolet resonance Raman spectra of hemoglobin excited at 200 and 218 nm: tertiary and quaternary structure differences Journal of the American Chemical Society. 107: 3370-3371. DOI: 10.1021/Ja00297A065 |
0.739 |
|
| 1985 |
Fodor SPA, Rava RP, Hays TR, Spiro TG. Ultraviolet resonance Raman spectroscopy of the nucleotides with 266-, 240-, 218-, and 200-nm pulsed laser excitation Journal of the American Chemical Society. 107: 1520-1529. DOI: 10.1021/Ja00292A012 |
0.361 |
|
| 1985 |
Rava RP, Spiro TG. Resonance enhancement in the ultraviolet Raman spectra of aromatic amino acids The Journal of Physical Chemistry. 89: 1856-1861. DOI: 10.1021/J100256A007 |
0.385 |
|
| 1985 |
Eng JF, Czernuszewicz RS, Spiro TG. Raman difference spectroscopy via backscattering from a spinning tube and from a low-temperature tuning fork Journal of Raman Spectroscopy. 16: 432-437. DOI: 10.1002/Jrs.1250160613 |
0.319 |
|
| 1985 |
Mitchell ML, Campbell DH, Traylor TG, Spiro TG. Molecular strain in chelated-heme complexes: Evidence from resonance Raman spectroscopy Inorganic Chemistry. 24: 967-971. DOI: 10.1002/Chin.198531290 |
0.375 |
|
| 1984 |
Woolery GL, Powers L, Winkler M, Solomon EI, Lerch K, Spiro TG. Extended X-ray absorption fine structure study of the coupled binuclear copper active site of tyrosinase from Neurospora crassa. Biochimica Et Biophysica Acta. 788: 155-61. PMID 6234942 DOI: 10.1016/0167-4838(84)90257-7 |
0.462 |
|
| 1984 |
Copeland RA, Fodor SPA, Spiro TG. Surface-enhanced Raman spectra of an active flavoenzyme: glucose oxidase and riboflavin binding protein on silver particles Journal of the American Chemical Society. 106: 3872-3874. DOI: 10.1021/Ja00325A034 |
0.32 |
|
| 1984 |
Woolery GL, Powers L, Winkler M, Solomon EI, Spiro TG. EXAFS studies of binuclear copper site of oxy-, deoxy-, and metaquo-, metfluoro-, and metazidohemocyanin from arthropods and molluscs Journal of the American Chemical Society. 106: 86-92. DOI: 10.1021/Ja00313A019 |
0.401 |
|
| 1984 |
Nestor L, Larrabee JA, Woolery G, Reinhammar B, Spiro TG. Resonance Raman spectra of blue copper proteins: assignments from normal mode calculations and copper-63/copper-65 and H2O/D2O shifts for stellacyanin and laccase Biochemistry. 23: 1084-1093. DOI: 10.1021/Bi00301A008 |
0.412 |
|
| 1984 |
Yamaguchi S, Spiro TG. Electronic and vibrational resonance Raman spectra of octamethyluranocene Chemical Physics Letters. 110: 209-213. DOI: 10.1016/0009-2614(84)80177-3 |
0.419 |
|
| 1984 |
Crisanti MA, Spiro TG, English DR, Hendrickson DN, Suslick KS. Resonance Raman spectra of high oxidation state iron porphyrin dimers Inorganic Chemistry. 23: 3897-3901. DOI: 10.1002/Chin.198513039 |
0.411 |
|
| 1984 |
Rava RP, Spiro TG. Selective enhancement of tyrosine and tryptophan resonance Raman spectra via ultraviolet laser excitation Journal of the American Chemical Society. 106: 4062-4064. DOI: 10.1002/Chin.198442045 |
0.409 |
|
| 1984 |
Benecky MJ, Dowling MG, Clarke MJ, Spiro TG. Resonance Raman spectra and structure of flavins bound to tetraammineruthenium(II) Inorganic Chemistry. 23: 865-869. DOI: 10.1002/Chin.198427044 |
0.433 |
|
| 1984 |
BENECKY MJ, DOWLING MG, CLARKE MJ, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA AND STRUCTURE OF FLAVINS BOUND TO TETRAAMMINERUTHENIUM(II) Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198427044 |
0.324 |
|
| 1984 |
STEIN P, ULMAN A, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF S2TPP, SSETPP, SE2TPP, AND H2TPP EXTENDED TETRAPHENYLPORPHINE VIBRATIONAL ASSIGNMENTS AND BONDING EFFECTS Chemischer Informationsdienst. 15. DOI: 10.1002/CHIN.198422052 |
0.352 |
|
| 1984 |
Stein P, Ulman A, Spiro TG. Resonance Raman spectra of S2TPP, SSeTPP, Se2TPP, and H2TPP extended tetraphenylporphine vibrational assignments and bonding effects The Journal of Physical Chemistry. 88: 369-374. DOI: 10.1002/Chin.198422052 |
0.459 |
|
| 1984 |
YACHANDRA VK, HARE J, GEWIRTH A, CZERNUSZEWICZ RS, KIMURA T, HOLM RH, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF SPINACH FERREDOXIN AND ADRENODOXIN AND OF ANALOG COMPLEXES Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198404043 |
0.571 |
|
| 1983 |
Benecky MJ, Copeland RA, Spiro TG. Resonance Raman spectra of flavin semiquinones stabilized by N5 methylation. Biochimica Et Biophysica Acta. 760: 163-8. PMID 6688536 DOI: 10.1016/0304-4165(83)90138-1 |
0.45 |
|
| 1983 |
Spiro TG, Terner J. Heme protein structure and dynamics, studied by Resonance Raman Spectroscopy Pure and Applied Chemistry. 55: 145-149. DOI: 10.1351/Pac198355010145 |
0.424 |
|
| 1983 |
Johnson MK, Czernuszewicz RS, Spiro TG, Fee JA, Sweeney WV. Resonance Raman spectroscopic evidence for a common [3-iron-4-sulfur] structure among proteins containing three-iron centers Journal of the American Chemical Society. 105: 6671-6678. DOI: 10.1021/Ja00360A022 |
0.348 |
|
| 1983 |
Yachandra V, Powers L, Spiro TG. X-ray absorption spectra and the coordination number of zinc and cobalt carbonic anhydrase as a function of pH and inhibitor binding Journal of the American Chemical Society. 105: 6596-6604. DOI: 10.1021/Ja00360A009 |
0.313 |
|
| 1983 |
Choi S, Lee JJ, Wei YH, Spiro TG. Resonance Raman and electronic spectra of heme a complexes and cytochrome oxidase Journal of the American Chemical Society. 105: 3692-3707. DOI: 10.1021/Ja00349A057 |
0.421 |
|
| 1983 |
Choi S, Spiro TG. Out-of-plane deformation modes in the resonance Raman spectra of metalloporphyrins and heme proteins Journal of the American Chemical Society. 105: 3683-3692. DOI: 10.1021/Ja00349A056 |
0.43 |
|
| 1983 |
Walters MA, Spiro TG, Scholler DM, Hoffman BH. Carp haemoglobin iron‐imidazole linkage and subunit equivalence; evidence from resonance Raman spectroscopy of deoxy‐ and nitrosyl forms Journal of Raman Spectroscopy. 14: 162-165. DOI: 10.1002/Jrs.1250140307 |
0.448 |
|
| 1983 |
Walters MA, Spiro TG. Resonance Raman enhancement of imidazole vibrations via charge-transfer transitions of pentacyanoiron(III) imidazole and imidazolate complexes Inorganic Chemistry. 22: 4014-4017. DOI: 10.1002/Chin.198413042 |
0.398 |
|
| 1983 |
Yachandra VK, Hare J, Gewirth A, Czernuszewicz RS, Kimura T, Holm RH, Spiro TG. Resonance Raman spectra of spinach ferredoxin and adrenodoxin and of analog complexes Journal of the American Chemical Society. 105: 6462-6469. DOI: 10.1002/Chin.198404043 |
0.617 |
|
| 1983 |
Yachandra VK, Hare J, Moura I, Spiro TG. Resonance Raman spectra of rubredoxin, desulforedoxin, and the synthetic analog Fe(S2-o-xyl)2: conformational effects Journal of the American Chemical Society. 105: 6455-6462. DOI: 10.1002/Chin.198404042 |
0.403 |
|
| 1983 |
CHOI S, SPIRO TG. ChemInform Abstract: OUT-OF-PLANE DEFORMATION MODES IN THE RESONANCE RAMAN SPECTRA OF METALLOPORPHYRINS AND HEME PROTEINS Chemischer Informationsdienst. 14. DOI: 10.1002/CHIN.198336051 |
0.323 |
|
| 1983 |
SPIRO TG. ChemInform Abstract: The Resonance Raman Spectroscopy of Metalloporphyrins and Heme Proteins (236 Literaturangaben). Chemischer Informationsdienst. 14. DOI: 10.1002/chin.198332364 |
0.322 |
|
| 1982 |
Walters MA, Spiro TG. Resonance Raman spectroscopic studies of axial ligation in oxyhemoglobin, oxymyoglobin, and nitrosylmyoglobin Biochemistry. 21: 6989-6995. PMID 7159577 DOI: 10.1021/Bi00269A057 |
0.41 |
|
| 1982 |
Choi S, Spiro TG, Langry KC, Smith KM, Budd DL, La Mar GN. Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins Journal of the American Chemical Society. 104: 4345-4351. DOI: 10.1021/Ja00380A006 |
0.427 |
|
| 1982 |
Choi S, Spiro TG, Langry KC, Smith KM. Vinyl influences on protoheme resonance Raman spectra: nickel(II) protoporphyrin IX with deuterated vinyl groups Journal of the American Chemical Society. 104: 4337-4344. DOI: 10.1021/Ja00380A005 |
0.414 |
|
| 1982 |
Terner J, Voss DF, Paddock C, Miles RB, Spiro TG. Picosecond resonance Raman spectrum of the oxyhemoglobin photoproduct. Evidence for an electronically excited state The Journal of Physical Chemistry. 86: 859-861. DOI: 10.1021/J100395A001 |
0.405 |
|
| 1982 |
Stein P, Terner J, Spiro TG. Hemoglobin R-state iron-imidazole frequency observed by time-resolved resonance Raman spectroscopy The Journal of Physical Chemistry. 86: 168-170. DOI: 10.1021/J100391A006 |
0.387 |
|
| 1982 |
CHOI S, SPIRO TG, LANGRY KC, SMITH KM, BUDD DL, LA MAR GN. ChemInform Abstract: STRUCTURAL CORRELATIONS AND VINYL INFLUENCES IN RESONANCE RAMAN SPECTRA OF PROTOHEME COMPLEXES AND PROTEINS Chemischer Informationsdienst. 13. DOI: 10.1002/chin.198246042 |
0.318 |
|
| 1981 |
Terner J, Stong JD, Spiro TG, Nagumo M, Nicol M, El-Sayed MA. Picosecond resonance Raman spectroscopic evidence for excited-state spin conversion in carbonmonoxy-hemoglobin photolysis. Proceedings of the National Academy of Sciences of the United States of America. 78: 1313-7. PMID 16592986 DOI: 10.1073/Pnas.78.3.1313 |
0.414 |
|
| 1981 |
Bowman WD, Spiro TG. Normal mode analysis of lumiflavin and interpretation of resonance Raman spectra of flavoproteins. Biochemistry. 20: 3313-8. PMID 7248286 DOI: 10.1021/Bi00514A051 |
0.422 |
|
| 1981 |
Spiro TG, Terner J. Hemoglobin photodynamics from resonance Raman spectroscopy Journal of Photochemistry. 17: 65. DOI: 10.1016/0047-2670(81)85134-9 |
0.431 |
|
| 1981 |
Stein P, Jensen PW, Spiro TG. Antisymmetric resonance Raman scattering from the breathing mode of CuBr2−4 Chemical Physics Letters. 80: 451-454. DOI: 10.1016/0009-2614(81)85055-5 |
0.383 |
|
| 1981 |
Spiro TG. Hemoglobin Structural Dynamics as Monitored by Resonance Raman Spectroscopy Israel Journal of Chemistry. 21: 81-86. DOI: 10.1002/Ijch.198100020 |
0.424 |
|
| 1981 |
WALTERS MA, SPIRO TG, SUSLICK KS, COLLMAN JP. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF (DIOXYGEN)(PORPHYRINATO)(HINDERED IMIDAZOLE)IRON(II) COMPLEXES: IMPLICATIONS FOR HEMOGLOBIN COOPERATIVITY Chemischer Informationsdienst. 12. DOI: 10.1002/Chin.198104048 |
0.427 |
|
| 1980 |
Dutta PK, Spencer R, Walsh C, Spiro TG. Resonance Raman and coherent anti-stokes Raman scattering spectra of flavin derivatives. Vibrational assignments and the zwitterionic structure of 8-methylamino-riboflavin. Biochimica Et Biophysica Acta. 623: 77-83. PMID 7378475 DOI: 10.1016/0005-2795(80)90009-4 |
0.607 |
|
| 1980 |
Dutta PK, Spiro TG. Resonance coherent anti-stokes Raman scattering spectra of oxidized and semiquinone forms of Clostridium MP flavodoxin Biochemistry. 19: 1590-1593. PMID 7378367 DOI: 10.1021/BI00549A009 |
0.544 |
|
| 1980 |
Dutta PK, Dallinger R, Spiro TG. Resonance CARS (coherent anti‐Stokes Raman scattering) line shapes via Frank–Condon scattering: Cytochrome c and β‐carotene The Journal of Chemical Physics. 73: 3580-3585. DOI: 10.1063/1.440582 |
0.579 |
|
| 1980 |
Stein P, Mitchell M, Spiro TG. Hydrogen-bond and deprotonation effects on the resonance Raman iron-imidazole mode in deoxyhemoglobin models: implications for hemoglobin cooperativity Journal of the American Chemical Society. 102: 7795-7797. DOI: 10.1021/Ja00546A035 |
0.384 |
|
| 1980 |
Walters MA, Spiro TG, Suslick KS, Collman JP. Resonance Raman spectra of (dioxygen)(porphyrinato)(hindered imidazole)iron(II) complexes: implications for hemoglobin cooperativity Journal of the American Chemical Society. 102: 6857-6858. DOI: 10.1021/Ja00542A037 |
0.424 |
|
| 1980 |
Stong JD, Burke JM, Daly P, Wright P, Spiro TG. Resonance Raman spectra of nitrosyl heme proteins and of porphyrin analogs Journal of the American Chemical Society. 102: 5815-5819. DOI: 10.1021/Ja00538A019 |
0.455 |
|
| 1980 |
Larrabee JA, Spiro TG. Structural studies of the hemocyanin active site. 2. Resonance Raman spectroscopy Journal of the American Chemical Society. 102: 4217-4223. DOI: 10.1021/Ja00532A038 |
0.386 |
|
| 1980 |
Terner J, Spiro TG, Nagumo M, Nicol MF, El-Sayed MA. Resonance Raman spectroscopy in the picosecond time scale: the carboxyhemoglobin photointermediate Journal of the American Chemical Society. 102: 3238-3239. DOI: 10.1021/Ja00529A056 |
0.394 |
|
| 1980 |
Bowman WD, Spiro TG. Fluorescence-free resonance Raman spectra of reduced nicotinamide adenine dinucleotide via ultraviolet excitation Journal of Raman Spectroscopy. 9: 369-371. DOI: 10.1002/Jrs.1250090605 |
0.468 |
|
| 1980 |
Stong JD, Spiro TG, Kubaska RJ, Shupack SI. Core-size marker resonance Raman bands of metallotetraphenylporphines Journal of Raman Spectroscopy. 9: 312-314. DOI: 10.1002/Jrs.1250090508 |
0.389 |
|
| 1980 |
Bowman WD, Spiro TG. MNDO–MOCIC evaluation of the uracil force field: Application to the interpretation of flavin vibrational spectra The Journal of Chemical Physics. 73: 5482-5492. DOI: 10.1002/Chin.198115100 |
0.325 |
|
| 1979 |
Spiro TG. Resonance Raman spectra of hemoproteins. Methods in Enzymology. 54: 233-49. PMID 732572 DOI: 10.1016/S0076-6879(78)54018-4 |
0.439 |
|
| 1979 |
Kincaid J, Stein P, Spiro TG. Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure. Proceedings of the National Academy of Sciences of the United States of America. 76: 549-52. PMID 284379 DOI: 10.1073/Pnas.76.2.549 |
0.429 |
|
| 1979 |
Larrabee JA, Spiro TG. Cobalt II substitution in the type 1 site of the multi-copper oxidase Rhus laccase. Biochemical and Biophysical Research Communications. 88: 753-60. PMID 157133 DOI: 10.1016/0006-291X(79)91472-4 |
0.321 |
|
| 1979 |
Wright PG, Stein P, Burke JM, Spiro TG. Resonance Raman spectra, excitation profiles and excited (iron .fwdarw. pyridine charge transfer) state geometry of bispyridine iron(II) heme Journal of the American Chemical Society. 101: 3531-3535. DOI: 10.1021/Ja00507A018 |
0.401 |
|
| 1979 |
Spiro TG, Stong JD, Stein P. Porphyrin core expansion and doming in heme proteins. New evidence from resonance Raman spectra of six-coordinate high-spin iron(III) hemes Journal of the American Chemical Society. 101: 2648-2655. DOI: 10.1021/Ja00504A027 |
0.403 |
|
| 1979 |
Salama S, Schugar H, Spiro TG. Resonance Raman spectroscopy of tetrahedral cobalt(II) thiourea and mercaptide complexes Inorganic Chemistry. 18: 104-107. DOI: 10.1002/Chin.197915042 |
0.402 |
|
| 1978 |
Dutta PK, Nestor J, Spiro TG. Resonance coherent anti-Stokes Raman scattering (CARS) spectra of flavin adenine dinucleotide, riboflavin binding protein and glucose oxidase. Biochemical and Biophysical Research Communications. 83: 209-16. PMID 697810 DOI: 10.1016/0006-291X(78)90418-7 |
0.6 |
|
| 1978 |
Salama S, Stong JD, Neilands JB, Spiro TG. Electronic and resonance Raman spectra of iron(III) complexes of enterobactin, catechol, and N-methyl-2,3-dihydroxybenzamide. Biochemistry. 17: 3781-5. PMID 151556 DOI: 10.1021/Bi00611A017 |
0.445 |
|
| 1978 |
Dutta PK, Spiro TG. Resonance CARS line shapes: Excited state parameters for flavin adenine dinucleotide The Journal of Chemical Physics. 69: 3119-3123. DOI: 10.1063/1.437004 |
0.549 |
|
| 1978 |
Dallinger RF, Stein P, Spiro TG. Resonance Raman spectroscopy of uranocene: observation of an anomalously polarized electronic band and assignment of energy levels Journal of the American Chemical Society. 100: 7865-7870. DOI: 10.1021/Ja00493A013 |
0.377 |
|
| 1978 |
Eickman NC, Solomon EI, Larrabee JA, Spiro TG, Lerch K. Ultraviolet resonance Raman study of oxytyrosinase. Comparison with oxyhemocyanins Journal of the American Chemical Society. 100: 6529-6531. DOI: 10.1021/Ja00488A059 |
0.546 |
|
| 1978 |
Dallinger RF, Nestor JR, Spiro TG. Resonance coherent anti-Stokes Raman scattering evidence for out-of-plane heme iron displacement within 6 ns of carbon monoxide dissociation in carbon monoxide hemoglobin Journal of the American Chemical Society. 100: 6251-6252. DOI: 10.1021/Ja00487A058 |
0.327 |
|
| 1978 |
Burke JM, Kincaid JR, Peters S, Gagne RR, Collman JP, Spiro TG. Structure-sensitive resonance Raman bands of tetraphenyl and "picket fence" porphyrin-iron complexes, including an oxyhemoglobin analog Journal of the American Chemical Society. 100: 6083-6088. DOI: 10.1021/Ja00487A018 |
0.403 |
|
| 1978 |
Burke JM, Kincaid JR, Spiro TG. Resonance Raman spectra and vibrational modes of iron(III) tetraphenylporphine .mu.-oxo dimer. Evidence for phenyl interaction and lack of dimer splitting Journal of the American Chemical Society. 100: 6077-6083. DOI: 10.1021/Ja00487A017 |
0.455 |
|
| 1978 |
Salama S, Spiro TG. Resonance Raman spectra of cobalt(II)-imidazole complexes: analogs of the binding site of cobalt-substituted zinc proteins Journal of the American Chemical Society. 100: 1105-1111. DOI: 10.1021/Ja00472A014 |
0.419 |
|
| 1978 |
Kincaid JR, Larrabee JA, Spiro TG. Resonance Raman spectra of copper(III) peptide complexes Journal of the American Chemical Society. 100: 334-336. DOI: 10.1021/Ja00469A083 |
0.384 |
|
| 1978 |
BURKE JM, KINCAID JR, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA AND VIBRATIONAL MODES OF IRON(III) TETRAPHENYLPORPHINE μ-OXO DIMER. EVIDENCE FOR PHENYL INTERACTION AND LACK OF DIMER SPLITTING Chemischer Informationsdienst. 9. DOI: 10.1002/chin.197852053 |
0.351 |
|
| 1978 |
SALAMA S, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF COBALT(II)-IMIDAZOLE COMPLEXES- ANALOGS OF THE BINDING SITE OF COBALT-SUBSTITUTED ZINC PROTEINS Chemischer Informationsdienst. 9. DOI: 10.1002/CHIN.197823045 |
0.307 |
|
| 1977 |
Dutta PK, Nestor JR, Spiro TG. Resonance coherent anti-Stokes Raman scattering spectra of fluorescent biological chromophores: Vibrational evidence for hydrogen bonding of flavin to glucose oxidase and for rapid solvent exchange. Proceedings of the National Academy of Sciences of the United States of America. 74: 4146-9. PMID 16592440 DOI: 10.1073/Pnas.74.10.4146 |
0.601 |
|
| 1977 |
Larrabee JA, Spiro TG, Ferris NS, Woodruff WH, Maltese WA, Kerr MS. Resonance raman study of mollusc and arthropod hemocyanins using ultraviolet excitation: copper environment and subunit inhomogeneity. Journal of the American Chemical Society. 99: 1979-80. PMID 839017 DOI: 10.1021/Ja00448A053 |
0.631 |
|
| 1977 |
Stein P, Brown JM, Spiro TG. Circularly polarized Raman spectra of IrCl62− and FeBr4−: Spin—orbit induced antisymmetry Chemical Physics. 25: 237-244. DOI: 10.1016/0301-0104(77)87079-1 |
0.376 |
|
| 1977 |
Salama S, Spiro TG. Visible and near-ultraviolet resonance Raman spectra of photolabile vitamin B12 derivatives with a rapid-flow technique Journal of Raman Spectroscopy. 6: 57-60. DOI: 10.1002/Jrs.1250060202 |
0.441 |
|
| 1976 |
Rakhit G, Spiro TG, Uyeda M. Resonance Raman evidence for Fe (IV) in compound II of horseradish peroxidase. Biochemical and Biophysical Research Communications. 71: 803-8. PMID 962956 DOI: 10.1016/0006-291X(76)90902-5 |
0.416 |
|
| 1976 |
Nestor J, Spiro TG, Klauminzer G. Coherent anti-Stokes Raman scattering (CARS) spectra, with resonance enhancement, of cytochrome c and vitamin B12 in dilute aqueous solution. Proceedings of the National Academy of Sciences of the United States of America. 73: 3329-32. PMID 185608 DOI: 10.1073/PNAS.73.10.3329 |
0.315 |
|
| 1976 |
Spiro TG, Burke JM. Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues. Journal of the American Chemical Society. 98: 5482-9. PMID 182734 DOI: 10.1021/Ja00434A013 |
0.409 |
|
| 1976 |
Stein P, Miskowski V, Woodruff WH, Griffin JP, Werner KG, Gaber BP, Spiro TG. Raman antiresonance: De‐enhancement of Raman intensity by forbidden electronic transitions The Journal of Chemical Physics. 64: 2159-2167. DOI: 10.1063/1.432438 |
0.589 |
|
| 1976 |
Spiro T. Resonance Raman spectroscopy Trends in Biochemical Sciences. 1: N109-N110. DOI: 10.1016/0968-0004(76)90312-1 |
0.426 |
|
| 1975 |
Rakshit G, Spiro TG. Resonance Raman spectra of horseradish peroxidase: evidence for anomalous heme structure. Biochemistry. 13: 5317-23. PMID 4433523 DOI: 10.1021/Bi00723A010 |
0.448 |
|
| 1975 |
Stein P, Burke JM, Spiro TG. Structural interpretation of heme protein resonance raman frequencies. Preliminary normal coordinate analysis results [25] Journal of the American Chemical Society. 97: 2304-2305. PMID 1133415 DOI: 10.1021/Ja00841A070 |
0.4 |
|
| 1975 |
Woodruff WH, Adams DH, Spiro TG, Yonetani T. Resonance Raman spectra of cobalt myoglobins and cobalt porphyrins. Evaluation of protein effects on porphyrin structure. Journal of the American Chemical Society. 97: 1695-8. PMID 1133400 DOI: 10.1021/Ja00840A012 |
0.646 |
|
| 1975 |
Tang SP, Spiro TG, Antanaitis C, Moss TH, Holm RH, Herskovitz T, Mortensen LE. Resonance Raman spectroscopic evidence for structural variation among bacterial ferredoxin, HiPIP, and Fe4S4(SCH2Ph)42. Biochemical and Biophysical Research Communications. 62: 1-6. PMID 1111508 DOI: 10.1016/S0006-291X(75)80396-2 |
0.43 |
|
| 1975 |
Miskowski V, Tang SP, Spiro TG, Shapiro E, Moss TH. The copper coordination group in "blue" copper proteins: evidence from resonance Raman spectra. Biochemistry. 14: 1244-50. PMID 804316 DOI: 10.1021/Bi00677A024 |
0.425 |
|
| 1975 |
Spiro TG. Resonance Raman spectroscopic studies of heme proteins. Biochimica Et Biophysica Acta. 416: 169-89. PMID 169917 DOI: 10.1016/0304-4173(75)90006-3 |
0.417 |
|
| 1975 |
Swanson BI, Rafalko JJ, Shriver DF, San Filippo J, Spiro TG. Raman spectroscopic identification of metal-metal stretching frequencies Inorganic Chemistry. 14: 1737-1738. DOI: 10.1021/Ic50149A068 |
0.493 |
|
| 1975 |
Strekas TC, Spiro TG. Resonance Raman spectra of superoxide-bridged binuclear complexes. .mu.-Superoxo-decacyanodicobaltate(5-) and .mu.-superoxo-decaamminedicobalt(5+) Inorganic Chemistry. 14: 1421-1423. DOI: 10.1021/Ic50148A047 |
0.422 |
|
| 1975 |
Keiderling TA, Wozniak WT, Gay RS, Jurkowitz D, Bernstein ER, Lippard SJ, Spiro TG. Raman and infrared spectra of hafnium tetrakis(tetrahydroborate) and hafnium tetrakis(tetrahydroborate-d16). Evidence for hafnium-boron bonding Inorganic Chemistry. 14: 576-579. DOI: 10.1021/Ic50145A027 |
0.382 |
|
| 1975 |
SWANSON BI, RAFALKO JJ, SHRIVER DF, SAN FILIPPO JJ, SPIRO TG. ChemInform Abstract: RAMAN SPECTROSCOPIC IDENTIFICATION OF METAL-METAL STRETCHING FREQUENCIES Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/CHIN.197537357 |
0.432 |
|
| 1975 |
STREKAS TC, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF SUPEROXIDE-BRIDGED BINUCLEAR COMPLEXES ((CN)5COO2CO(CN)5)(5-) AND ((NH3)5COO2CO(NH3)5)(5+) Chemischer Informationsdienst. 6. DOI: 10.1002/Chin.197533348 |
0.427 |
|
| 1975 |
STEIN P, BURKE JM, SPIRO TG. ChemInform Abstract: STRUCTURAL INTERPRETATION OF HEME PROTEIN RESONANCE RAMAN FREQUENCIES, PRELIMINARY NORMAL COORDINATE ANALYSIS RESULTS Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/Chin.197527069 |
0.405 |
|
| 1975 |
WOODRUFF WH, ADAMS DH, SPIRO TG, YONETANI T. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF COBALT MYOGLOBINS AND COBALT PORPHYRINS, EVALUATION OF PROTEIN EFFECTS ON PORPHYRIN STRUCTURE Chemischer Informationsdienst. 6. DOI: 10.1002/CHIN.197524061 |
0.323 |
|
| 1975 |
KEIDERLING TA, WOZNIAK WT, GAY RS, JURKOWITZ D, BERNSTEIN ER, LIPPARD SJ, SPIRO TG. ChemInform Abstract: RAMAN AND INFRARED SPECTRA OF HF(BH4)4 AND HF(BD4)4, EVIDENCE FOR HF-B BONDING Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/Chin.197521015 |
0.358 |
|
| 1975 |
GABER BP, MISKOWSKI V, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SCATTERING FROM IRON(III)- AND COPPER(II)-TRANSFERRIN AND AN IRON(III) MODEL COMPOUND. A SPECTROSCOPIC INTERPRETATION OF THE TRANSFERRIN BINDING SITE Chemischer Informationsdienst. 6. DOI: 10.1002/Chin.197502389 |
0.348 |
|
| 1974 |
Woodruff WH, Spiro TG, Yonetani T. Resonance Raman spectra of cobalt-substituted hemoglobin: cooperativity and displacement of the cobalt atom upon oxygenation. Proceedings of the National Academy of Sciences of the United States of America. 71: 1065-9. PMID 4524615 DOI: 10.1073/Pnas.71.4.1065 |
0.617 |
|
| 1974 |
Gaber BP, Miskowski V, Spiro TG. Resonance Raman scattering from iron(3)- and copper(II)-transferrin and an iron(3) model compound. A spectroscopic interpretation of the transferrin binding site. Journal of the American Chemical Society. 96: 6868-73. PMID 4436502 DOI: 10.1021/Ja00829A010 |
0.34 |
|
| 1974 |
Strekas TC, Spiro TG. Resonance-raman evidence for anomalous heme structures in cytochrome c' from Rhodopseudomonas palustris. Biochimica Et Biophysica Acta. 351: 237-45. PMID 4366150 DOI: 10.1016/0005-2795(74)90186-X |
0.354 |
|
| 1974 |
Spiro TG, Strekas TC. Resonance Raman spectra of heme proteins. Effects of oxidation and spin state. Journal of the American Chemical Society. 96: 338-45. PMID 4361043 DOI: 10.1002/Chin.197414064 |
0.382 |
|
| 1974 |
Woodruff WH, Spiro TG, Gilvarg C. Raman spectroscopy in vivo: evidence on the structure of dipicolinate in intact spores of Bacillus megaterium. Biochemical and Biophysical Research Communications. 58: 197-203. PMID 4208642 DOI: 10.1016/0006-291X(74)90911-5 |
0.608 |
|
| 1974 |
Woodruff WH, Spiro TG. A Circulating Sample Cell for Temperature Control in Resonance Raman Spectroscopy Applied Spectroscopy. 28: 74-75. DOI: 10.1366/000370274774332993 |
0.582 |
|
| 1974 |
Strekas TC, Adams DH, Packer A, Spiro TG. Absorption Corrections and Concentration Optimization for Absorbing Samples in Resonance Raman Spectroscopy Applied Spectroscopy. 28: 324-327. DOI: 10.1366/000370274774332353 |
0.374 |
|
| 1974 |
Woodruff WH, Spiro TG. Resonance Raman Spectroscopy of Reaction Intermediates by a Rapid Mixing, Continuous Flow Technique Applied Spectroscopy. 28: 576-578. DOI: 10.1366/000370274774331886 |
0.588 |
|
| 1974 |
Terzis A, Strekas TC, Spiro TG. Raman spectra and metal-metal bonding in the molecules trimethyl germane-, trimethyl stannane-, trichloro germane-, or trichlorostannane-pentacarbonylmanganese, or -pentacarbonylrhenium Inorganic Chemistry. 13: 1346-1349. DOI: 10.1021/Ic50136A020 |
0.314 |
|
| 1974 |
Scovell WM, Spiro TG. Vibrational and Raman intensity analysis of a ferredoxin model, dithiodiiron hexacarbonyl Inorganic Chemistry. 13: 304-308. DOI: 10.1021/Ic50132A011 |
0.376 |
|
| 1974 |
Spiro TG. Resonance Raman spectroscopy. New structure probe for biological chromophores Accounts of Chemical Research. 7: 339-344. DOI: 10.1021/Ar50082A004 |
0.395 |
|
| 1974 |
SCOVELL WM, SPIRO TG. ChemInform Abstract: VIBRATIONAL AND RAMAN INTENSITY ANALYSIS OF A FERREDOXIN MODEL, S2FE2(CO)6 Chemischer Informationsdienst. 5. DOI: 10.1002/Chin.197415383 |
0.38 |
|
| 1973 |
Tang SP, Spiro TG, Mukai K, Kimura T. Resonance Raman scattering and optical absorption of adrenodoxin and selena-adrenodoxin. Biochemical and Biophysical Research Communications. 53: 869-74. PMID 4738718 DOI: 10.1016/0006-291X(73)90173-3 |
0.383 |
|
| 1973 |
Wozniak WT, Spiro TG. Resonance Raman spectra of vitamin B 12 derivatives. Journal of the American Chemical Society. 95: 3402-4. PMID 4708830 DOI: 10.1021/Ja00791A065 |
0.37 |
|
| 1973 |
Kubas GT, Spiro TG, Terzis A. A novel compound with a planar Fe-S-S-Fe bridge and its possible relation to ferredoxins. Journal of the American Chemical Society. 95: 273-4. PMID 4682896 DOI: 10.1021/Ja00782A065 |
0.53 |
|
| 1973 |
Kubas GJ, Spiro TG. Resonance Raman spectra of tetracarbonyldi-.mu.-2,2,5,5-tetramethylhex-3-yne-diiron. Stretching vibration of an iron-iron double bond Inorganic Chemistry. 12: 1797-1801. DOI: 10.1021/Ic50126A018 |
0.635 |
|
| 1973 |
Sommer BA, Margerum DW, Renner J, Saltman P, Spiro TG. Reactivity and aging in hydroxy-iron(III) polymers, analogs of ferritin cores Bioinorganic Chemistry. 2: 295-309. DOI: 10.1016/S0006-3061(00)80202-1 |
0.49 |
|
| 1973 |
Nestro J, Spiro TG. Circularly polarized Raman spectroscopy: Direct determination of antisymmetric scattering in the resonance Raman spectrum of ferrocytochrome c Journal of Raman Spectroscopy. 1: 539-550. DOI: 10.1002/Jrs.1250010604 |
0.363 |
|
| 1973 |
Strekas TC, Spiro TG. Hemoglobin resonance Raman excitation profiles with a tunable dye laser Journal of Raman Spectroscopy. 1: 387-392. DOI: 10.1002/Jrs.1250010411 |
0.439 |
|
| 1973 |
Strekas TC, Packer AJ, Spiro TG. Resonance Raman spectra of ferri-hemoglobin fluoride: Three scattering regimes Journal of Raman Spectroscopy. 1: 197-206. DOI: 10.1002/Jrs.1250010207 |
0.451 |
|
| 1973 |
KUBAS GJ, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF TETRACARBONYLDI-MU-2,2,5,5-TETRAMETHYLHEX-3-YNE-DIIRON, STRETCHING VIBRATION OF AN IRON-IRON-DOUBLE BOND Chemischer Informationsdienst. 4: no-no. DOI: 10.1002/CHIN.197339348 |
0.597 |
|
| 1973 |
WOZNIAK WT, SPIRO TG. ChemInform Abstract: RESONANCE RAMAN SPECTRA OF VITAMIN B12 DERIVATIVES Chemischer Informationsdienst. 4: no-no. DOI: 10.1002/Chin.197330067 |
0.373 |
|
| 1972 |
Strekas TC, Spiro TG. Hemoglobin: resonance Raman spectra. Biochimica Et Biophysica Acta. 263: 830-3. PMID 5034222 DOI: 10.1016/0005-2795(72)90072-4 |
0.457 |
|
| 1972 |
Spiro TG, Strekas TC. Resonance Raman spectra of hemoglobin and cytochrome c: inverse polarization and vibronic scattering. Proceedings of the National Academy of Sciences of the United States of America. 69: 2622-6. PMID 4506783 DOI: 10.1073/Pnas.69.9.2622 |
0.432 |
|
| 1972 |
Strekas TC, Spiro TG. Cytochrome c: resonance Raman spectra. Biochimica Et Biophysica Acta. 278: 188-92. PMID 4341727 DOI: 10.1016/0005-2795(72)90121-3 |
0.417 |
|
| 1971 |
Spiro TG, Terzis A. Raman intensities and bond orders in the hexacarbonyls of chromium, molybdenum, and tungsten Inorganic Chemistry. 10: 643-645. DOI: 10.1021/Ic50097A042 |
0.324 |
|
| 1971 |
Spiro TG, Bulliner PA, Quicksall CO. Raman spectra and metal-metal bond strengths for hexaphenylditin and hexaphenyldilead Inorganic Chemistry. 10: 13-18. DOI: 10.1021/Ic50095A004 |
0.309 |
|
| 1971 |
Spiro TG, Fontal B. Raman spectra and metal-metal bonds. Force constants and bond polarizability derivatives for hexamethyldisilicon, -germanium, -tin, and -lead Inorganic Chemistry. 10: 9-13. DOI: 10.1021/Ic50095A003 |
0.32 |
|
| 1971 |
TERZIS A, SPIRO TG. ChemInform Abstract: RAMAN-INTENSITAETEN UND BINDUNGSORDNUNG VON CHROM-, MOLYBDAEN- UND WOLFRAMHEXACARBONYL Chemischer Informationsdienst. Organische Chemie. 2: no-no. DOI: 10.1002/Chin.197119079 |
0.37 |
|
| 1971 |
TERZIS A, RAYMOND KN, SPIRO TG. ChemInform Abstract: QUADRATISCH-PYRAMIDALE STRUKTUR VON (NI(CN)5)(3-) (RAMAN-, IR- UND ROENTGENUNTERSUCHUNG) Chemischer Informationsdienst. Organische Chemie. 2: no-no. DOI: 10.1002/Chin.197102049 |
0.338 |
|
| 1970 |
Terzis A, Spiro TG. The Raman spectrum of (C<inf>5</inf>H<inf>5</inf>)Fe(CO)<inf>4</inf>: A Resonance Effect Journal of the Chemical Society D: Chemical Communications. DOI: 10.1039/C2970001160B |
0.363 |
|
| 1970 |
Bulliner PA, Maroni VA, Spiro TG. Raman and infrared frequencies, force constants, and bond polarizability derivatives for trimethylplatinum hydroxide, chloride, and iodide Inorganic Chemistry. 9: 1887-1898. DOI: 10.1021/Ic50090A019 |
0.341 |
|
| 1970 |
Bulliner P, Spiro TG. Alternate force fields in the normal coordinate analysis of the bridged polynuclear metal atom complexes Bi6(OH)126+, Pb4(OH)44+ and Tl4(OEt)4 Spectrochimica Acta Part a: Molecular Spectroscopy. 26: 1641-1650. DOI: 10.1016/0584-8539(70)80226-4 |
0.301 |
|
| 1970 |
BULLINER PA, MARONI VICTOR A, SPIRO TG. ChemInform Abstract: RAMAN- UND INFRAROTFREQUENZEN, KRAFTKONSTANTEN UND BINDUNGSPOLARISIERBARKEITEN VON TETRAMEREM HYDROXO-, CHLORO- UND JODO-TRIMETHYL-PLATIN(IV) (I) Chemischer Informationsdienst. Organische Chemie. 1: no-no. DOI: 10.1002/Chin.197041127 |
0.372 |
|
| 1969 |
Farrell FJ, Maroni VA, Spiro TG. Vibrational analysis for Nb6O198- and Ta6O198- and the the Raman intensity criterion for metal-metal interaction Inorganic Chemistry. 8: 2638-2642. DOI: 10.1021/Ic50082A019 |
0.303 |
|
| 1968 |
Maroni VA, Spiro TG. Raman and infrared spectra of tetrameric thallium(I) alkoxides and their analysis Inorganic Chemistry. 7: 193-197. DOI: 10.1021/Ic50060A003 |
0.421 |
|
| 1968 |
Maroni VA, Spiro TG. Vibrational analysis for polynuclear hydroxylead(II) complexes Inorganic Chemistry. 7: 188-192. DOI: 10.1021/Ic50060A002 |
0.331 |
|
| 1967 |
Maroni VA, Spiro TG. Vibrational Spectra of Polynuclear Hydroxy Complexes of Lead(II) Journal of the American Chemical Society. 89: 45-48. DOI: 10.1021/Ja00977A009 |
0.391 |
|
| 1967 |
Spiro TG. Raman and infrared spectra of crystalline halothallates Inorganic Chemistry. 6: 569-572. DOI: 10.1021/Ic50049A031 |
0.423 |
|
| 1966 |
Maroni VA, Spiro TG. The vibrational spectrum of the hydrolytic hexamer of bismuth 3. Journal of the American Chemical Society. 88: 1410-2. PMID 5914522 DOI: 10.1021/Ja00959A015 |
0.38 |
|
| 1966 |
Quicksall CO, Spiro TG. Raman Spectra of Tetrahalozincates and the Structure of Aqueous ZnCl42 Inorganic Chemistry. 5: 2232-2233. DOI: 10.1021/Ic50046A034 |
0.415 |
|
| 1965 |
Spiro TG. Raman Spectra of Crystalline Chlorothallates Inorganic Chemistry. 4: 1290-1293. DOI: 10.1021/Ic50031A013 |
0.424 |
|
| 1963 |
Spiro TG, Hume DN. Mixed ligand complex formation in lead-chloride-bromide solutions Inorganic Chemistry. 2: 863-864. DOI: 10.1021/Ic50008A049 |
0.554 |
|
| 1963 |
Spiro TG, Hume DN. A spectrophotometric study of the saturated mixed complexes of mercury(II)-bromide-iodide Inorganic Chemistry. 2: 340-345. DOI: 10.1021/Ic50006A025 |
0.556 |
|
| 1961 |
Spiro TG, Hume DN. The uncharged mixed halides of mercury(II). Equilibrium constants and ultraviolet spectra Journal of the American Chemical Society. 83: 4305-4310. DOI: 10.1021/Ja01482A001 |
0.586 |
|
| Show low-probability matches. |
