| Year |
Citation |
Score |
| 2022 |
Collins DP, Johnson E, Coulter ED, Beharry Z, Ballou DP, Dawson JH. Caught in the act: Monitoring OO bond cleavage in Acylperoxoferric cytochrome P450cam to form compound I in real time. Journal of Inorganic Biochemistry. 111949. PMID 36028338 DOI: 10.1016/j.jinorgbio.2022.111949 |
0.706 |
|
| 2018 |
Sono M, Sun S, Modi A, Hargrove MS, Molitor B, Frankenberg-Dinkel N, Dawson JH. Spectroscopic evidence supporting neutral thiol ligation to ferrous heme iron. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 30251130 DOI: 10.1007/S00775-018-1611-3 |
0.822 |
|
| 2015 |
Draganova EB, Akbas N, Adrian SA, Lukat-Rodgers GS, Collins DP, Dawson JH, Allen CE, Schmitt MP, Rodgers KR, Dixon DW. Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment. Biochemistry. 54: 6598-609. PMID 26478504 DOI: 10.1021/Acs.Biochem.5B00666 |
0.736 |
|
| 2015 |
Beltrán J, Kloss B, Hosler JP, Geng J, Liu A, Modi A, Dawson JH, Sono M, Shumskaya M, Ampomah-Dwamena C, Love JD, Wurtzel ET. Control of carotenoid biosynthesis through a heme-based cis-trans isomerase. Nature Chemical Biology. 11: 598-605. PMID 26075523 DOI: 10.1038/Nchembio.1840 |
0.793 |
|
| 2015 |
Modi AR, Dawson JH. Oxidizing intermediates in p450 catalysis: a case for multiple oxidants. Advances in Experimental Medicine and Biology. 851: 63-81. PMID 26002731 DOI: 10.1007/978-3-319-16009-2_2 |
0.801 |
|
| 2015 |
Smith AD, Modi AR, Sun S, Dawson JH, Wilks A. Spectroscopic Determination of Distinct Heme Ligands in Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa. Biochemistry. 54: 2601-12. PMID 25849630 DOI: 10.1021/Acs.Biochem.5B00017 |
0.784 |
|
| 2014 |
Wang C, Lovelace LL, Sun S, Dawson JH, Lebioda L. Structures of K42N and K42Y sperm whale myoglobins point to an inhibitory role of distal water in peroxidase activity. Acta Crystallographica. Section D, Biological Crystallography. 70: 2833-9. PMID 25372675 DOI: 10.1107/S1399004714017787 |
0.818 |
|
| 2014 |
Davydov R, Laryukhin M, Ledbetter-Rogers A, Sono M, Dawson JH, Hoffman BM. Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediates. Biochemistry. 53: 4894-903. PMID 25046203 DOI: 10.1021/Bi500296D |
0.336 |
|
| 2014 |
Sun S, Sono M, Du J, Dawson JH. Evidence of the direct involvement of the substrate TCP radical in functional switching from oxyferrous O2 carrier to ferric peroxidase in the dual-function hemoglobin/dehaloperoxidase from Amphitrite ornata. Biochemistry. 53: 4956-69. PMID 24972312 DOI: 10.1021/Bi5002757 |
0.819 |
|
| 2014 |
Sun S, Sono M, Wang C, Du J, Lebioda L, Dawson JH. Influence of heme environment structure on dioxygen affinity for the dual function Amphitrite ornata hemoglobin/dehaloperoxidase. Insights into the evolutional structure-function adaptations. Archives of Biochemistry and Biophysics. 545: 108-15. PMID 24440609 DOI: 10.1016/J.Abb.2014.01.010 |
0.795 |
|
| 2014 |
Zhong F, Lisi GP, Collins DP, Dawson JH, Pletneva EV. Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins. Proceedings of the National Academy of Sciences of the United States of America. 111: E306-15. PMID 24398520 DOI: 10.1073/Pnas.1317173111 |
0.822 |
|
| 2013 |
Wang C, Lovelace LL, Sun S, Dawson JH, Lebioda L. Complexes of dual-function hemoglobin/dehaloperoxidase with substrate 2,4,6-trichlorophenol are inhibitory and indicate binding of halophenol to compound I. Biochemistry. 52: 6203-10. PMID 23952341 DOI: 10.1021/Bi400627W |
0.806 |
|
| 2013 |
Sun Y, Zeng W, Benabbas A, Ye X, Denisov I, Sligar SG, Du J, Dawson JH, Champion PM. Investigations of heme ligation and ligand switching in cytochromes p450 and p420. Biochemistry. 52: 5941-51. PMID 23905516 DOI: 10.1021/Bi400541V |
0.572 |
|
| 2013 |
Molitor B, Stassen M, Modi A, El-Mashtoly SF, Laurich C, Lubitz W, Dawson JH, Rother M, Frankenberg-Dinkel N. A heme-based redox sensor in the methanogenic archaeon Methanosarcina acetivorans. The Journal of Biological Chemistry. 288: 18458-72. PMID 23661702 DOI: 10.1074/Jbc.M113.476267 |
0.816 |
|
| 2013 |
Sun S, Sono M, Dawson JH. Mono- and bis-phosphine-ligated H93G myoglobin: spectral models for ferrous-phosphine and ferrous-CO cytochrome P450. Journal of Inorganic Biochemistry. 127: 238-45. PMID 23639797 DOI: 10.1016/J.Jinorgbio.2013.03.006 |
0.831 |
|
| 2013 |
Davydov R, Dawson JH, Perera R, Hoffman BM. The use of deuterated camphor as a substrate in (1)H ENDOR studies of hydroxylation by cryoreduced oxy P450cam provides new evidence of the involvement of compound I. Biochemistry. 52: 667-71. PMID 23215047 DOI: 10.1021/Bi301527C |
0.567 |
|
| 2013 |
Collins DP, Isaac IS, Coulter ED, Hager PW, Ballou DP, Dawson JH. Reaction of ferric Caldariomyces fumago chloroperoxidase with meta-chloroperoxybenzoic acid: Journal of Porphyrins and Phthalocyanines. 17: 63-72. DOI: 10.1142/S1088424612501234 |
0.804 |
|
| 2013 |
Collins DP, Dawson JH. Recent History of Heme-Containing Proteins: Advances in Structure, Functions, and Reaction Intermediate Determination Comprehensive Inorganic Chemistry Ii (Second Edition): From Elements to Applications. 3: 65-102. DOI: 10.1016/B978-0-08-097774-4.00306-5 |
0.648 |
|
| 2012 |
Huang X, Wang C, Celeste LR, Lovelace LL, Sun S, Dawson JH, Lebioda L. Complex of myoglobin with phenol bound in a proximal cavity. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68: 1465-71. PMID 23192025 DOI: 10.1107/S1744309112045514 |
0.808 |
|
| 2012 |
Sumithran S, Sono M, Raner GM, Dawson JH. Single turnover studies of oxidative halophenol dehalogenation by horseradish peroxidase reveal a mechanism involving two consecutive one electron steps: toward a functional halophenol bioremediation catalyst. Journal of Inorganic Biochemistry. 117: 316-21. PMID 23102773 DOI: 10.1016/J.Jinorgbio.2012.09.017 |
0.782 |
|
| 2012 |
Hannibal L, Collins D, Brassard J, Chakravarti R, Vempati R, Dorlet P, Santolini J, Dawson JH, Stuehr DJ. Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 51: 8514-29. PMID 22957700 DOI: 10.1021/Bi300863A |
0.734 |
|
| 2012 |
Owens CP, Du J, Dawson JH, Goulding CW. Characterization of heme ligation properties of Rv0203, a secreted heme binding protein involved in Mycobacterium tuberculosis heme uptake. Biochemistry. 51: 1518-31. PMID 22283334 DOI: 10.1021/Bi2018305 |
0.562 |
|
| 2011 |
Bandara DM, Sono M, Bruce GS, Brash AR, Dawson JH. Coordination modes of tyrosinate-ligated catalase-type heme enzymes: magnetic circular dichroism studies of Plexaura homomalla allene oxide synthase, Mycobacterium avium ssp. paratuberculosis protein-2744c, and bovine liver catalase in their ferric and ferrous states. Journal of Inorganic Biochemistry. 105: 1786-94. PMID 22104301 DOI: 10.1016/J.Jinorgbio.2011.09.026 |
0.461 |
|
| 2011 |
Du J, Huang X, Sun S, Wang C, Lebioda L, Dawson JH. Amphitrite ornata dehaloperoxidase (DHP): investigations of structural factors that influence the mechanism of halophenol dehalogenation using "peroxidase-like" myoglobin mutants and "myoglobin-like" DHP mutants. Biochemistry. 50: 8172-80. PMID 21800850 DOI: 10.1021/Bi2009129 |
0.815 |
|
| 2011 |
Du J, Sono M, Dawson JH. The H93G Myoglobin Cavity Mutant as a Versatile Scaffold for Modeling Heme Iron Coordination Structures in Protein Active Sites and Their Characterization with Magnetic Circular Dichroism Spectroscopy. Coordination Chemistry Reviews. 255: 700-716. PMID 21423881 DOI: 10.1016/J.Ccr.2011.01.029 |
0.584 |
|
| 2011 |
Sivaramakrishnan S, Ouellet H, Du J, McLean KJ, Medzihradszky KF, Dawson JH, Munro AW, Ortiz de Montellano PR. A novel intermediate in the reaction of seleno CYP119 with m-chloroperbenzoic acid. Biochemistry. 50: 3014-24. PMID 21381758 DOI: 10.1021/Bi101728Y |
0.598 |
|
| 2011 |
Du J, Perera R, Dawson JH. Alkylamine-ligated H93G myoglobin cavity mutant: a model system for endogenous lysine and terminal amine ligation in heme proteins such as nitrite reductase and cytochrome f. Inorganic Chemistry. 50: 1242-9. PMID 21250678 DOI: 10.1021/Ic101644U |
0.725 |
|
| 2011 |
Perera R, Sono M, Voegtle HL, Dawson JH. Molecular basis for the inability of an oxygen atom donor ligand to replace the natural sulfur donor heme axial ligand in cytochrome P450 catalysis. Spectroscopic characterization of the Cys436Ser CYP2B4 mutant. Archives of Biochemistry and Biophysics. 507: 119-25. PMID 21147058 DOI: 10.1016/J.Abb.2010.12.010 |
0.836 |
|
| 2011 |
Perera R, Sono M, Kinloch R, Zhang H, Tarasev M, Im SC, Waskell L, Dawson JH. Stabilization and spectroscopic characterization of the dioxygen complex of wild-type cytochrome P4502B4 (CYP2B4) and its distal side E301Q, T302A and proximal side F429H mutants at subzero temperatures. Biochimica Et Biophysica Acta. 1814: 69-75. PMID 20637316 DOI: 10.1016/J.Bbapap.2010.07.012 |
0.818 |
|
| 2011 |
Du J, Sono M, Dawson JH. Ferric His93Gly myoglobin cavity mutant and its complexes with thioether and selenolate as heme protein models Journal of Porphyrins and Phthalocyanines. 15: 29-38. DOI: 10.1142/S1088424610002872 |
0.581 |
|
| 2010 |
Davydov R, Osborne RL, Shanmugam M, Du J, Dawson JH, Hoffman BM. Probing the oxyferrous and catalytically active ferryl states of Amphitrite ornata dehaloperoxidase by cryoreduction and EPR/ENDOR spectroscopy. Detection of compound I. Journal of the American Chemical Society. 132: 14995-5004. PMID 20925340 DOI: 10.1021/Ja1059747 |
0.732 |
|
| 2010 |
Du J, Sono M, Dawson JH. Functional switching of Amphitrite ornata dehaloperoxidase from O2-binding globin to peroxidase enzyme facilitated by halophenol substrate and H2O2. Biochemistry. 49: 6064-9. PMID 20565134 DOI: 10.1021/Bi100741Z |
0.51 |
|
| 2010 |
Airola MV, Du J, Dawson JH, Crane BR. Heme binding to the Mammalian circadian clock protein period 2 is nonspecific. Biochemistry. 49: 4327-38. PMID 20411915 DOI: 10.1021/Bi901945W |
0.497 |
|
| 2010 |
Kinloch RD, Sono M, Sudhamsu J, Crane BR, Dawson JH. Magnetic circular dichroism spectroscopic characterization of the NOS-like protein from Geobacillus stearothermophilus (gsNOS). Journal of Inorganic Biochemistry. 104: 357-64. PMID 20110129 DOI: 10.1016/J.Jinorgbio.2009.12.014 |
0.82 |
|
| 2009 |
Droghetti E, Sumithran S, Sono M, Antalík M, Fedurco M, Dawson JH, Smulevich G. Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH. Archives of Biochemistry and Biophysics. 489: 68-75. PMID 19622342 DOI: 10.1016/J.Abb.2009.07.008 |
0.771 |
|
| 2009 |
Osborne RL, Coggins MK, Raner GM, Walla M, Dawson JH. The mechanism of oxidative halophenol dehalogenation by Amphitrite ornata dehaloperoxidase is initiated by H2O2 binding and involves two consecutive one-electron steps: role of ferryl intermediates. Biochemistry. 48: 4231-8. PMID 19371065 DOI: 10.1021/Bi900367E |
0.7 |
|
| 2009 |
Vetter SW, Terentis AC, Osborne RL, Dawson JH, Goodin DB. Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 179-91. PMID 18923851 DOI: 10.1007/S00775-008-0436-X |
0.69 |
|
| 2008 |
Davydov R, Osborne RL, Kim SH, Dawson JH, Hoffman BM. EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl hemes. Biochemistry. 47: 5147-55. PMID 18407661 DOI: 10.1021/Bi702514D |
0.682 |
|
| 2008 |
Gruia F, Ionascu D, Kubo M, Ye X, Dawson J, Osborne RL, Sligar SG, Denisov I, Das A, Poulos TL, Terner J, Champion PM. Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy. Biochemistry. 47: 5156-67. PMID 18407660 DOI: 10.1021/Bi7025485 |
0.662 |
|
| 2008 |
Spolitak T, Dawson JH, Ballou DP. Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 599-611. PMID 18273651 DOI: 10.1007/S00775-008-0348-9 |
0.427 |
|
| 2008 |
Sook BR, Block DR, Sumithran S, Montañez GE, Rodgers KR, Dawson JH, Eichenbaum Z, Dixon DW. Characterization of SiaA, a streptococcal heme-binding protein associated with a heme ABC transport system. Biochemistry. 47: 2678-88. PMID 18247478 DOI: 10.1021/Bi701604Y |
0.793 |
|
| 2008 |
Du J, Sono M, Dawson JH. The proximal and distal pockets of the H93G myoglobin cavity mutant bind identical ligands with different affinities: Quantitative analysis of imidazole and pyridine binding Spectroscopy. 22: 123-141. DOI: 10.3233/Spe-2008-0330 |
0.529 |
|
| 2008 |
Gruia F, Ionascu D, Kubo M, Ye X, Dawson J, Osborne RL, Sligar SG, Denisov I, Das A, Poulos TL, Terner J, Champion PM. Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy (Biochemistry (2008) 47, 18, (5156-5167)) Biochemistry. 47: 9344. DOI: 10.1021/Bi801317Z |
0.596 |
|
| 2008 |
Pond AE, Ledbetter AP, Sono M, Goodin DB, Dawson JH. Redox Enzymes: Correlation of Three-Dimensional Structure and Mechanism for Heme-Containing Oxygenases and Peroxidases Electron Transfer in Chemistry. 3: 56-104. DOI: 10.1002/9783527618248.ch36 |
0.788 |
|
| 2007 |
Osborne RL, Coggins MK, Terner J, Dawson JH. Caldariomyces fumago chloroperoxidase catalyzes the oxidative dehalogenation of chlorophenols by a mechanism involving two one-electron steps. Journal of the American Chemical Society. 129: 14838-9. PMID 17990879 DOI: 10.1021/Ja0746969 |
0.689 |
|
| 2007 |
Denisov IG, Dawson JH, Hager LP, Sligar SG. The ferric-hydroperoxo complex of chloroperoxidase. Biochemical and Biophysical Research Communications. 363: 954-8. PMID 17920039 DOI: 10.1016/J.Bbrc.2007.09.085 |
0.426 |
|
| 2007 |
Osborne RL, Coggins MK, Walla M, Dawson JH. Horse heart myoglobin catalyzes the H2O2-dependent oxidative dehalogenation of chlorophenols to DNA-binding radicals and quinones. Biochemistry. 46: 9823-9. PMID 17676875 DOI: 10.1021/Bi700684U |
0.705 |
|
| 2007 |
Dawson JH, Gray HB. Preface. Preface for Stiefel Issue Journal of Inorganic Biochemistry. 101: 1543. DOI: 10.1016/J.Jinorgbio.2007.08.004 |
0.33 |
|
| 2007 |
Perera R, Jin S, Sono M, Dawson JH. Cytochrome P450-catalyzed hydroxylations and epoxidations Metal Ions in Life Sciences. 3: 319-359. DOI: 10.1002/9780470028155.Ch11 |
0.656 |
|
| 2007 |
Kinloch RD, Dawson JH. Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation Chemtracts. 20: 94-101. |
0.778 |
|
| 2007 |
Sumithran S, Dawson JH. Characterization of the heme binding properties of Staphylococcus aureus IsdA Chemtracts. 20: 69-77. |
0.741 |
|
| 2006 |
Spolitak T, Dawson JH, Ballou DP. Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: nature and possible function of compound ES. Journal of Inorganic Biochemistry. 100: 2034-44. PMID 17095096 DOI: 10.1016/J.Jinorgbio.2006.09.026 |
0.436 |
|
| 2006 |
Raner GM, Thompson JI, Haddy A, Tangham V, Bynum N, Ramachandra Reddy G, Ballou DP, Dawson JH. Spectroscopic investigations of intermediates in the reaction of cytochrome P450(BM3)-F87G with surrogate oxygen atom donors. Journal of Inorganic Biochemistry. 100: 2045-53. PMID 17083977 DOI: 10.1016/J.Jinorgbio.2006.09.025 |
0.41 |
|
| 2006 |
Zhuang J, Amoroso JH, Kinloch R, Dawson JH, Baldwin MJ, Gibney BR. Evaluation of electron-withdrawing group effects on heme binding in designed proteins: implications for heme a in cytochrome c oxidase. Inorganic Chemistry. 45: 4685-94. PMID 16749832 DOI: 10.1021/Ic060072C |
0.817 |
|
| 2006 |
Kim SH, Perera R, Hager LP, Dawson JH, Hoffman BM. Rapid freeze-quench ENDOR study of chloroperoxidase compound I: the site of the radical. Journal of the American Chemical Society. 128: 5598-9. PMID 16637602 DOI: 10.1021/Ja060776L |
0.651 |
|
| 2006 |
Osborne RL, Sumithran S, Coggins MK, Chen YP, Lincoln DE, Dawson JH. Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties. Journal of Inorganic Biochemistry. 100: 1100-8. PMID 16603247 DOI: 10.1016/J.Jinorgbio.2006.02.008 |
0.827 |
|
| 2006 |
Qin J, Perera R, Lovelace LL, Dawson JH, Lebioda L. Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins. Biochemistry. 45: 3170-7. PMID 16519512 DOI: 10.1021/Bi052171S |
0.632 |
|
| 2006 |
Osborne RL, Raner GM, Hager LP, Dawson JH. C. fumago chloroperoxidase is also a dehaloperoxidase: oxidative dehalogenation of halophenols. Journal of the American Chemical Society. 128: 1036-7. PMID 16433494 DOI: 10.1021/Ja056213B |
0.684 |
|
| 2005 |
Kim SH, Yang TC, Perera R, Jin S, Bryson TA, Sono M, Davydov R, Dawson JH, Hoffman BM. Cryoreduction EPR and 13C, 19F ENDOR study of substrate-bound substates and solvent kinetic isotope effects in the catalytic cycle of cytochrome P450cam and its T252A mutant. Dalton Transactions (Cambridge, England : 2003). 3464-9. PMID 16234926 DOI: 10.1039/B506764M |
0.701 |
|
| 2005 |
Perera R, Sono M, Raner GM, Dawson JH. Subzero-temperature stabilization and spectroscopic characterization of homogeneous oxyferrous complexes of the cytochrome P450 BM3 (CYP102) oxygenase domain and holoenzyme. Biochemical and Biophysical Research Communications. 338: 365-71. PMID 16197919 DOI: 10.1016/J.Bbrc.2005.08.078 |
0.622 |
|
| 2005 |
Eakanunkul S, Lukat-Rodgers GS, Sumithran S, Ghosh A, Rodgers KR, Dawson JH, Wilks A. Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae. Biochemistry. 44: 13179-91. PMID 16185086 DOI: 10.1021/Bi050422R |
0.8 |
|
| 2005 |
Glascock MC, Ballou DP, Dawson JH. Direct observation of a novel perturbed oxyferrous catalytic intermediate during reduced putidaredoxin-initiated turnover of cytochrome P-450-CAM: probing the effector role of putidaredoxin in catalysis. The Journal of Biological Chemistry. 280: 42134-41. PMID 16115886 DOI: 10.1074/Jbc.M505426200 |
0.81 |
|
| 2005 |
Fedurco M, Augustynski J, Indiani C, Smulevich G, Antalík M, Bánó M, Sedlák E, Glascock MC, Dawson JH. Electrochemistry of unfolded cytochrome c in neutral and acidic urea solutions. Journal of the American Chemical Society. 127: 7638-46. PMID 15898816 DOI: 10.1021/ja050321g |
0.802 |
|
| 2005 |
Spolitak T, Dawson JH, Ballou DP. Reaction of ferric cytochrome P450cam with peracids: kinetic characterization of intermediates on the reaction pathway. The Journal of Biological Chemistry. 280: 20300-9. PMID 15781454 DOI: 10.1074/Jbc.M501761200 |
0.432 |
|
| 2005 |
Sono M, Perera R, Jin S, Makris TM, Sligar SG, Bryson TA, Dawson JH. The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM. Archives of Biochemistry and Biophysics. 436: 40-9. PMID 15752707 DOI: 10.1016/J.Abb.2004.12.026 |
0.71 |
|
| 2005 |
Davydov R, Perera R, Jin S, Yang TC, Bryson TA, Sono M, Dawson JH, Hoffman BM. Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy. Journal of the American Chemical Society. 127: 1403-13. PMID 15686372 DOI: 10.1021/Ja045351I |
0.678 |
|
| 2004 |
Zhuang J, Amoroso JH, Kinloch R, Dawson JH, Baldwin MJ, Gibney BR. Design of a five-coordinate heme protein maquette: a spectroscopic model of deoxymyoglobin. Inorganic Chemistry. 43: 8218-20. PMID 15606161 DOI: 10.1021/Ic048502R |
0.818 |
|
| 2004 |
Fedurco M, Augustynski J, Indiani C, Smulevich G, Antalík M, Bánó M, Sedlák E, Glascock MC, Dawson JH. The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies. Biochimica Et Biophysica Acta. 1703: 31-41. PMID 15588700 DOI: 10.1016/J.Bbapap.2004.09.013 |
0.803 |
|
| 2004 |
Ogura H, Nishida CR, Hoch UR, Perera R, Dawson JH, Ortiz de Montellano PR. EpoK, a cytochrome P450 involved in biosynthesis of the anticancer agents epothilones A and B. Substrate-mediated rescue of a P450 enzyme. Biochemistry. 43: 14712-21. PMID 15544342 DOI: 10.1021/Bi048980D |
0.609 |
|
| 2004 |
Osborne RL, Taylor LO, Han KP, Ely B, Dawson JH. Amphitrite ornata dehaloperoxidase: enhanced activity for the catalytically active globin using MCPBA. Biochemical and Biophysical Research Communications. 324: 1194-8. PMID 15504340 DOI: 10.1016/J.Bbrc.2004.09.174 |
0.672 |
|
| 2004 |
Jin S, Bryson TA, Dawson JH. Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 644-53. PMID 15365901 DOI: 10.1007/S00775-004-0575-7 |
0.56 |
|
| 2004 |
Green MT, Dawson JH, Gray HB. Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry. Science (New York, N.Y.). 304: 1653-6. PMID 15192224 DOI: 10.1126/Science.1096897 |
0.598 |
|
| 2004 |
Perera R, Dawson JH. Modeling heme protein active sites with the his93gly cavity mutant of sperm whale myoglobin: Complexes with nitrogen-, oxygen- and sulfur-donor proximal ligands Journal of Porphyrins and Phthalocyanines. 8: 246-254. DOI: 10.1142/S1088424604000234 |
0.659 |
|
| 2004 |
Anzenbacher P, Dawson JH. Advances in the inorganic biochemistry of cytochrome P450, nitric oxide synthase and related systems Journal of Inorganic Biochemistry. 98: v. DOI: 10.1016/J.Jinorgbio.2004.06.002 |
0.31 |
|
| 2004 |
Ohashi M, Koshiyama T, Ueno T, Yanase M, Fujii H, Watanabe Y, Osborne RL, Dawson JH. Preparation of artificial metalloenzymes by insertion of chromium (III) Schiff base complexes into apomyoglobin mutants Chemtracts. 17: 359-365. |
0.621 |
|
| 2004 |
Osborne RL, Dawson JH. Spectroscopic Characterization and Ligand-Binding Properties of Chlorite Dismutase from the Chlorate Respiring Bacterial Strain GR-I Chemtracts. 17: 36-45. |
0.618 |
|
| 2003 |
Perera R, Sono M, Sigman JA, Pfister TD, Lu Y, Dawson JH. Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction. Proceedings of the National Academy of Sciences of the United States of America. 100: 3641-6. PMID 12655049 DOI: 10.1073/Pnas.0737142100 |
0.7 |
|
| 2003 |
Jin S, Makris TM, Bryson TA, Sligar SG, Dawson JH. Epoxidation of olefins by hydroperoxo-ferric cytochrome P450. Journal of the American Chemical Society. 125: 3406-7. PMID 12643683 DOI: 10.1021/Ja029272N |
0.575 |
|
| 2003 |
Voegtle HL, Sono M, Adak S, Pond AE, Tomita T, Perera R, Goodin DB, Ikeda-Saito M, Stuehr DJ, Dawson JH. Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase. Biochemistry. 42: 2475-84. PMID 12600215 DOI: 10.1021/Bi0271502 |
0.824 |
|
| 2003 |
Bryson TA, Gibson JM, Stewart JJ, Voegtle H, Tiwari A, Dawson JH, Marley W, Harmon B. Synthesis of quinolines, pyridine ligands and biological probes in green media Green Chemistry. 5: 177-180. DOI: 10.1039/B211968D |
0.771 |
|
| 2003 |
Dawson JH, Jin S, Lamczyk MC, Voegde HL, Bryson TA. Oxygen activation by cytochrome P450 and nitric oxide synthase. Evidence for a second active oxidant from studies using P450-CAM as a model system Journal of Inorganic Biochemistry. 96: 33. DOI: 10.1016/S0162-0134(03)80459-2 |
0.529 |
|
| 2002 |
Dmochowski IJ, Dunn AR, Wilker JJ, Crane BR, Green MT, Dawson JH, Sligar SG, Winkler JR, Gray HB. Sensitizer-linked substrates and ligands: ruthenium probes of cytochrome P450 structure and mechanism. Methods in Enzymology. 357: 120-33. PMID 12424904 DOI: 10.1016/S0076-6879(02)57672-2 |
0.815 |
|
| 2002 |
Davydov R, Ledbetter-Rogers A, Martásek P, Larukhin M, Sono M, Dawson JH, Masters BS, Hoffman BM. EPR and ENDOR characterization of intermediates in the cryoreduced oxy-nitric oxide synthase heme domain with bound L-arginine or N(G)-hydroxyarginine. Biochemistry. 41: 10375-81. PMID 12173923 DOI: 10.1021/Bi0260637 |
0.414 |
|
| 2002 |
Dawson JH, Pond AE, Roach MP. H93G myoglobin cavity mutant as versatile template for modeling heme proteins: magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes. Biopolymers. 67: 200-6. PMID 12012432 DOI: 10.1002/Bip.10087 |
0.464 |
|
| 2001 |
Abraham BD, Sono M, Boutaud O, Shriner A, Dawson JH, Brash AR, Gaffney BJ. Characterization of the coral allene oxide synthase active site with UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy: evidence for tyrosinate ligation to the ferric enzyme heme iron. Biochemistry. 40: 2251-9. PMID 11329294 DOI: 10.1021/Bi002121H |
0.456 |
|
| 2001 |
Voegtle H, Dawson JH. Effect of distal cavity mutations on the formation of compound I in catalase-peroxidases Chemtracts. 14: 12-17. |
0.756 |
|
| 2000 |
Coulter ED, Cheek J, Ledbetter AP, Chang CK, Dawson JH. Preparation and initial characterization of the compound I, II, and III states of iron methylchlorin-reconstituted horseradish peroxidase and myoglobin: models for key intermediates in iron chlorin enzymes. Biochemical and Biophysical Research Communications. 279: 1011-5. PMID 11162466 DOI: 10.1006/Bbrc.2000.4077 |
0.806 |
|
| 2000 |
Pond AE, Roach MP, Thomas MR, Boxer SG, Dawson JH. The H93G myoglobin cavity mutant as a versatile template for modeling heme proteins: ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity. Inorganic Chemistry. 39: 6061-6. PMID 11151505 DOI: 10.1021/Ic0007198 |
0.442 |
|
| 1999 |
Das TK, Franzen S, Pond A, Dawson JH, Rousseau DL. Formation of a Five-Coordinate Hydroxide-Bound Heme in the His93Gly Mutant of Sperm Whale Myoglobin. Inorganic Chemistry. 38: 1952-1953. PMID 11670970 DOI: 10.1021/Ic990049+ |
0.367 |
|
| 1999 |
Isaac IS, Dawson JH. Haem iron-containing peroxidases. Essays in Biochemistry. 34: 51-69. PMID 10730188 DOI: 10.1042/Bse0340051 |
0.824 |
|
| 1999 |
Dawson J, Knowles RG. A microtiter-plate assay of nitric oxide synthase activity Molecular Biotechnology. 12: 275-279. PMID 10631684 DOI: 10.1385/Mb:12:3:275 |
0.33 |
|
| 1999 |
Sono M, Ledbetter AP, McMillan K, Roman LJ, Shea TM, Masters BS, Dawson JH. Essential thiol requirement to restore pterin- or substrate-binding capability and to regenerate native enzyme-type high-spin heme spectra in the Escherichia coli-expressed tetrahydrobiopterin-free oxygenase domain of neuronal nitric oxide synthase. Biochemistry. 38: 15853-62. PMID 10625450 DOI: 10.1021/Bi991580J |
0.792 |
|
| 1999 |
Pond AE, Sono M, Elenkova EA, McRee DE, Goodin DB, English AM, Dawson JH. Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH. Journal of Inorganic Biochemistry. 76: 165-74. PMID 10605835 DOI: 10.1016/S0162-0134(99)00112-9 |
0.427 |
|
| 1999 |
Pond AE, Sono M, Elenkova EA, Goodin DB, English AM, Dawson JH. Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase. Biospectroscopy. 5: S42-52. PMID 10512537 DOI: 10.1002/(Sici)1520-6343(1999)5:5+3.0.Co;2-9 |
0.435 |
|
| 1999 |
Cheek J, Mandelman D, Poulos TL, Dawson JH. A study of the K(+)-site mutant of ascorbate peroxidase: mutations of protein residues on the proximal side of the heme cause changes in iron ligation on the distal side. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 4: 64-72. PMID 10499104 DOI: 10.1007/S007750050290 |
0.429 |
|
| 1999 |
Sigman JA, Pond AE, Dawson JH, Lu Y. Engineering cytochrome c peroxidase into cytochrome P450: a proximal effect on heme-thiolate ligation. Biochemistry. 38: 11122-9. PMID 10460168 DOI: 10.1021/Bi990815O |
0.549 |
|
| 1999 |
Ledbetter AP, McMillan K, Roman LJ, Masters BS, Dawson JH, Sono M. Low-temperature stabilization and spectroscopic characterization of the dioxygen complex of the ferrous neuronal nitric oxide synthase oxygenase domain. Biochemistry. 38: 8014-21. PMID 10387045 DOI: 10.1021/Bi990619H |
0.8 |
|
| 1999 |
Pond AE, Roach MP, Sono M, Rux AH, Franzen S, Hu R, Thomas MR, Wilks A, Dou Y, Ikeda-Saito M, Ortiz de Montellano PR, Woodruff WH, Boxer SG, Dawson JH. Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism. Biochemistry. 38: 7601-8. PMID 10360958 DOI: 10.1021/Bi9825448 |
0.399 |
|
| 1999 |
Roach MP, Pond AE, Thomas MR, Boxer SG, Dawson JH. The role of the distal and proximal protein environments in controlling the ferric spin state and in stabilizing thiolate ligation in heme systems: Thiolate adducts of the myoglobin H93G cavity mutant Journal of the American Chemical Society. 121: 12088-12093. DOI: 10.1021/Ja9915504 |
0.427 |
|
| 1999 |
Wilker JJ, Dmochowski IJ, Dawson JH, Winkler JR, Gray HB. Substrates for Rapid Delivery of Electrons and Holes to Buried Active Sites in Proteins Angewandte Chemie. 38: 89-92. DOI: 10.1002/(Sici)1521-3773(19990115)38:1/2<89::Aid-Anie89>3.0.Co;2-R |
0.734 |
|
| 1999 |
Wilker JJ, Dmochowski IJ, Dawson JH, Winkler JR, Gray HB. Substrate für schnelle Ladungsübertragung auf redoxaktive Cofaktoren in den aktiven Zentren von Proteinen Angewandte Chemie. 111: 93-96. DOI: 10.1002/(Sici)1521-3757(19990115)111:1/2<93::Aid-Ange93>3.0.Co;2-P |
0.749 |
|
| 1999 |
Vlcek A. J, Wilker JJ, Dmochowski IJ, Dawson JH, Winkler JR, Gray HB. Substrates for rapid delivery of electrons and holes to buried active sites in proteins Chemtracts. 12: 565-569. |
0.739 |
|
| 1999 |
Vlcek A. J, Wilker JJ, Dmochowski IJ, Dawson JH, Winkler JR, Gray HB. Substrates for rapid delivery of electrons and holes to buried active sites in proteins Chemtracts. 12: 565-569. |
0.739 |
|
| 1998 |
Cheek J, Low DW, Gray HB, Dawson JH. Histidine-tailed microperoxidase-10: a pH-dependent ligand switch. Biochemical and Biophysical Research Communications. 253: 195-8. PMID 9878514 DOI: 10.1006/Bbrc.1998.9778 |
0.481 |
|
| 1998 |
Franzen S, Roach MP, Chen YP, Dyer RB, Woodruff WH, Dawson JH. The unusual reactivities of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase do not arise from a histidine imidazolate proximal heme iron ligand Journal of the American Chemical Society. 120: 4658-4661. DOI: 10.1021/Ja973212D |
0.489 |
|
| 1998 |
Pond AE, Bruce GS, English AM, Sono M, Dawson JH. Spectroscopic study of the compound ES and the oxoferryl compound II states of cytochrome c peroxidase: Comparison with the compound II of horseradish peroxidase Inorganica Chimica Acta. 275: 250-255. DOI: 10.1016/S0020-1693(97)06106-9 |
0.389 |
|
| 1997 |
Roach MP, Chen YP, Woodin SA, Lincoln DE, Lovell CR, Dawson JH. Notomastus lobatus chloroperoxidase and Amphitrite ornata dehaloperoxidase both contain histidine as their proximal heme iron ligand. Biochemistry. 36: 2197-202. PMID 9047320 DOI: 10.1021/Bi9621371 |
0.48 |
|
| 1997 |
Roach MP, Franzen S, Pang PS, Boxer SG, Woodruff WH, Dawson JH. Thiolate adducts of cavity mutant myoglobin H93G as models for cytochrome P450 Journal of Inorganic Biochemistry. 67: 134. DOI: 10.1016/S0162-0134(97)80014-1 |
0.304 |
|
| 1997 |
Wilker JJ, Dmochowski IJ, Dawson JH, Winkler JR, Gray HH. Production of high valent iron-oxo species in cytochrome P450-CAM by electron transfer through protein substrates Faseb Journal. 11: A808. |
0.768 |
|
| 1997 |
Dmochowski LJ, Wilker JJ, Dawson JH, Winkler JR, Gray HB. Photo-induced electron injection into cytochrome P450CAM via sensitizer-tethered substrates: A pathway to compound I? Faseb Journal. 11: A808. |
0.647 |
|
| 1996 |
Zhang E, Chen YP, Roach MP, Lincoln DE, Lovell CR, Woodin SA, Dawson JH, Lebioda L. Crystallization and initial spectroscopic characterization of the heme-containing dehaloperoxidase from the marine polychaete Amphitrite ornata. Acta Crystallographica. Section D, Biological Crystallography. 52: 1191-3. PMID 15299583 DOI: 10.1107/S0907444996007974 |
0.322 |
|
| 1996 |
Sono M, Roach MP, Coulter ED, Dawson JH. Heme-Containing Oxygenases. Chemical Reviews. 96: 2841-2888. PMID 11848843 DOI: 10.1021/Cr9500500 |
0.411 |
|
| 1996 |
Blanke SR, Martinis SA, Sligar SG, Hager LP, Rux JJ, Dawson JH. Probing the heme iron coordination structure of alkaline chloroperoxidase. Biochemistry. 35: 14537-43. PMID 8931550 DOI: 10.1021/Bi961512M |
0.494 |
|
| 1996 |
Martinis SA, Blanke SR, Hager LP, Sligar SG, Hoa GH, Rux JJ, Dawson JH. Probing the heme iron coordination structure of pressure-induced cytochrome P420cam. Biochemistry. 35: 14530-6. PMID 8931549 DOI: 10.1021/Bi961511U |
0.482 |
|
| 1996 |
Hawkins BK, Wilks A, Powers LS, Ortiz de Montellano PR, Dawson JH. Ligation of the iron in the heme-heme oxygenase complex: X-ray absorption, electronic absorption and magnetic circular dichroism studies. Biochimica Et Biophysica Acta. 1295: 165-73. PMID 8695642 DOI: 10.1016/0167-4838(96)00031-3 |
0.821 |
|
| 1996 |
Dawson J. Enzyme Frontiers. (Book Reviews: Cytochrome P450. Structure, Mechanism, and Biochemistry.) Science. 271: 1507-1508. DOI: 10.1126/Science.271.5255.1507 |
0.323 |
|
| 1996 |
Cheek J, Coulter ED, Maritano S, Marchesini A, Dawson JH. Characterization of a plant paraperoxidase from Curcurbita pepo using magnetic circular dichroism: Direct evidence for cyanide ligation in the ferric resting state Inorganica Chimica Acta. 243: 317-325. DOI: 10.1016/0020-1693(95)04922-3 |
0.469 |
|
| 1995 |
Liu HI, Sono M, Kadkhodayan S, Hager LP, Hedman B, Hodgson KO, Dawson JH. X-ray absorption near edge studies of cytochrome P-450-CAM, chloroperoxidase, and myoglobin. Direct evidence for the electron releasing character of a cysteine thiolate proximal ligand. The Journal of Biological Chemistry. 270: 10544-50. PMID 7737989 DOI: 10.1074/Jbc.270.18.10544 |
0.436 |
|
| 1995 |
Burstyn JN, Yu AE, Dierks EA, Hawkins BK, Dawson JH. Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme. Biochemistry. 34: 5896-903. PMID 7727447 DOI: 10.1021/Bi00017A019 |
0.826 |
|
| 1995 |
Sono M, Stuehr DJ, Ikeda-Saito M, Dawson JH. Identification of nitric oxide synthase as a thiolate-ligated heme protein using magnetic circular dichroism spectroscopy. Comparison with cytochrome P-450-CAM and chloroperoxidase. The Journal of Biological Chemistry. 270: 19943-8. PMID 7544348 DOI: 10.1074/Jbc.270.34.19943 |
0.432 |
|
| 1995 |
Kadkhodayan S, Coulter ED, Maryniak DM, Bryson TA, Dawson JH. Uncoupling oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450-CAM. Direct observation of an intermolecular isotope effect for substrate C-H activation. The Journal of Biological Chemistry. 270: 28042-8. PMID 7499289 DOI: 10.1074/Jbc.270.47.28042 |
0.333 |
|
| 1995 |
Coulter ED, Sono M, Chang CK, Lopez O, Dawson JH. Electron paramagnetic resonance spectroscopy as a probe of coordination structure in green heme systems: iron chlorins and iron formylporphyrins reconstituted into myoglobin Inorganica Chimica Acta. 240: 603-608. DOI: 10.1016/0020-1693(95)04588-0 |
0.401 |
|
| 1994 |
Hawkins BK, Hilgen-Willis S, Pielak GJ, Dawson JH. Novel axial ligand interchange in cytochrome c: Incorporation of a histidine at position 82 leads to displacement of the wild-type methionine-80 ligand Journal of the American Chemical Society. 116: 3111-3112. DOI: 10.1021/Ja00086A046 |
0.793 |
|
| 1994 |
Bracete AM, Kadkhodayan S, Sono M, Huff AM, Zhuang C, Cooper DK, Smith KM, Chang CK, Dawson JH. Iron chlorin-reconstituted histidine-ligated heme proteins as models for naturally occurring iron chlorin proteins: Magnetic circular dichroism spectroscopy as a probe of iron chlorin coordination structure Inorganic Chemistry. 33: 5042-5049. DOI: 10.1021/Ic00100A032 |
0.421 |
|
| 1994 |
Kintner ET, Nardo JV, Dawson JH. Magnetic circular dichroism spectroscopy of zinc(II) tetraphenylporphyrin-ligand complexes: The effect of the axial ligand on spectral properties Spectrochimica Acta Part a: Molecular Spectroscopy. 50: 493-507. DOI: 10.1016/0584-8539(94)80164-9 |
0.403 |
|
| 1993 |
Huff AM, Chang CK, Cooper DK, Smith KM, Dawson JH. Imidazole- and alkylamine-ligated iron(II, III) chlorin complexes as models for histidine and lysine coordination to iron in dibydroporphyrin-containing proteins: Characterization with magnetic circular dichroism spectroscopy Inorganic Chemistry. 32: 1460-1466. DOI: 10.1021/Ic00060A023 |
0.41 |
|
| 1993 |
Pascher T, Dawson J, Winkler J, Gray H. Photoinduced electron transfer to cytochrome P450cam. Journal of Inorganic Biochemistry. 51: 234. DOI: 10.1016/0162-0134(93)85268-D |
0.566 |
|
| 1992 |
Dawson JH, Kadkhodayan S, Zhuang C, Sono M. On the use of iron octa-alkylporphyrins as models for protoporphyrin IX-containing heme systems in studies employing magnetic circular dichroism spectroscopy. Journal of Inorganic Biochemistry. 45: 179-92. PMID 1634892 DOI: 10.1016/0162-0134(92)80043-U |
0.397 |
|
| 1992 |
Hawkins BK, Dawson JH. Intrasubstituent isotope effect studies of oxidative N-demethylations catalyzed by secondary amine monooxygenase. Comparison to cytochrome P-450 Journal of the American Chemical Society. 114: 3547-3549. DOI: 10.1021/Ja00035A059 |
0.798 |
|
| 1991 |
Bracete AM, Sono M, Dawson JH. Effects of cyanogen bromide modification of the distal histidine on the spectroscopic and ligand binding properties of myoglobin: magnetic circular dichroism spectroscopy as a probe of distal water ligation in ferric high-spin histidine-bound heme proteins. Biochimica Et Biophysica Acta. 1080: 264-70. PMID 1954234 DOI: 10.1016/0167-4838(91)90012-O |
0.455 |
|
| 1991 |
Dawson JH, Bracete AM, Huff AM, Kadkhodayan S, Zeitler CM, Sono M, Chang CK, Loewen PC. The active site structure of E. coli HPII catalase. Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron. Febs Letters. 295: 123-6. PMID 1662642 DOI: 10.1016/0014-5793(91)81401-S |
0.44 |
|
| 1991 |
Sono M, Bracete AM, Huff AM, Ikeda-Saito M, Dawson JH. Evidence that a formyl-substituted iron porphyrin is the prosthetic group of myeloperoxidase: magnetic circular dichroism similarity of the peroxidase to Spirographis heme-reconstituted myoglobin. Proceedings of the National Academy of Sciences of the United States of America. 88: 11148-52. PMID 1662385 DOI: 10.1073/Pnas.88.24.11148 |
0.447 |
|
| 1991 |
Rux JJ, Dawson JH. Magnetic circular dichroism spectroscopy as a probe of axial heme ligand replacement in semisynthetic mutants of cytochrome c. Febs Letters. 290: 49-51. PMID 1655536 DOI: 10.1016/0014-5793(91)81222-T |
0.446 |
|
| 1991 |
Sono M, Hager LP, Dawson JH. Electron paramagnetic resonance investigations of exogenous ligand complexes of low-spin ferric chloroperoxidase: further support for endogenous thiolate ligation to the heme iron. Biochimica Et Biophysica Acta. 1078: 351-9. PMID 1650250 DOI: 10.1016/0167-4838(91)90156-T |
0.468 |
|
| 1991 |
Kintner ET, Dawson JH. Spectroscopic studies of ferric porphyrins with quantum mechanically admixed intermediate-spin states: Models for cytochrome c′ Inorganic Chemistry. 30: 4892-4897. DOI: 10.1021/Ic00026A009 |
0.364 |
|
| 1991 |
Hawkins BK, Dawson JH. Secondary amine mono-oxygenase: Looks like myoglobin, acts like cytochrome P-450. Mechanistic studies of oxidative N-demethylation. Journal of Inorganic Biochemistry. 43: 342. DOI: 10.1016/0162-0134(91)84329-8 |
0.79 |
|
| 1989 |
Svastits EW, Alberta JA, Kim IC, Dawson JH. Magnetic circular dichroism studies of the active site structure of hemoprotein H-450: comparison to cytochrome P-450 and sensitivity to pH effects. Biochemical and Biophysical Research Communications. 165: 1170-6. PMID 2610685 DOI: 10.1016/0006-291X(89)92725-3 |
0.405 |
|
| 1989 |
Alberta JA, Andersson LA, Dawson JH. Spectroscopic characterization of secondary amine mono-oxygenase. Comparison to cytochrome P-450 and myoglobin. The Journal of Biological Chemistry. 264: 20467-73. PMID 2555360 |
0.399 |
|
| 1989 |
Anzenbacher P, Dawson JH, Kitagawa T. Towards a unified concept of oxygen activation by heme enzymes: the role of the proximal ligand Journal of Molecular Structure. 214: 149-158. DOI: 10.1016/0022-2860(89)80011-0 |
0.424 |
|
| 1989 |
Crull GB, Nardo JV, Dawson JH. Direct observation of substrate binding to ferrous-CO cytochrome P-450-CAM using 19F NMR Febs Letters. 254: 39-42. DOI: 10.1016/0014-5793(89)81005-1 |
0.424 |
|
| 1988 |
Dawson JH. Probing structure-function relations in heme-containing oxygenases and peroxidases. Science (New York, N.Y.). 240: 433-9. PMID 3358128 DOI: 10.1126/Science.3358128 |
0.439 |
|
| 1988 |
Nardo JV, Sono M, Dawson JH. Magnetic circular dichroism studies of a thiolate complex of zinc protoporphyrin. A non-iron hyperporphyrin model for ferrous-CO cytochrome P-450 Inorganica Chimica Acta. 151: 173-175. DOI: 10.1016/S0020-1693(00)83462-3 |
0.378 |
|
| 1987 |
Alberta JA, Dawson JH. Purification to homogeneity and initial physical characterization of secondary amine monooxygenase. The Journal of Biological Chemistry. 262: 11857-63. PMID 3624236 |
0.332 |
|
| 1987 |
Dawson JH, Sono M. Cytochrome P-450 and chloroperoxidase: Thiolate-ligated heme enzymes. Spectroscopic determination of their active site structures and mechanistic implications of thiolate ligation Chemical Reviews. 87: 1255-1276. DOI: 10.1021/Cr00081A015 |
0.379 |
|
| 1986 |
Penner-Hahn JE, Smith Eble K, McMurry TJ, Renner M, Balch AL, Groves JT, Dawson JH, Hodgson KO. Structural characterization of horseradish peroxidase using EXAFS spectroscopy. Evidence for Fe = O ligation in compounds I and II. Journal of the American Chemical Society. 108: 7819-25. PMID 22283292 DOI: 10.1021/Ja00284A054 |
0.391 |
|
| 1986 |
Sono M, Dawson JH, Hall K, Hager LP. Ligand and halide binding properties of chloroperoxidase: peroxidase-type active site heme environment with cytochrome P-450 type endogenous axial ligand and spectroscopic properties. Biochemistry. 25: 347-56. PMID 3955002 |
0.4 |
|
| 1986 |
Sono M, Dawson JH, Ikeda-Saito M. Characterization of the spleen green hemeprotein with magnetic and natural circular dichroism spectroscopy: positive evidence for a myeloperoxidase-type active site. Biochimica Et Biophysica Acta. 873: 62-72. PMID 3017435 DOI: 10.1016/0167-4838(86)90190-1 |
0.406 |
|
| 1986 |
KAU L, SVASTITS EW, SONO M, DAWSON JH, HODGSON KO. EXAFS STUDY OF ACTIVE INTERMEDIATES : HEME ENZYMES AND MODEL COMPOUNDS Le Journal De Physique Colloques. 47: C8-1151-C8-1154. DOI: 10.1051/Jphyscol:19868224 |
0.438 |
|
| 1986 |
Dawson JH, Kau LS, Penner-Hahn JE, Sono M, Eble KS, Bruce GS, Hager LP, Hodgson KO. Oxygenated cytochrome P-450-CAM and chloroperoxidase: direct evidence for sulfur donor ligation trans to dioxygen and structural characterization using EXAFS spectroscopy Journal of the American Chemical Society. 108: 8114-8116. DOI: 10.1021/Ja00285A052 |
0.36 |
|
| 1986 |
Kau LS, Svastits EW, Dawson JH, Hodgson KO. Iron-sulfur bond lengths in ferrous-carbonyl heme complexes as a function of sulfur donor type Inorganic Chemistry. 25: 4307-4309. DOI: 10.1021/Ic00243A047 |
0.424 |
|
| 1986 |
Svastits EW, Dawson JH. Models for ferrous cytochrome b5: Sign inversions in the magnetic circular dichroism spectra of bis-imidazole ferrous porphyrin systems Inorganica Chimica Acta. 123: 83-86. DOI: 10.1016/S0020-1693(00)84305-4 |
0.399 |
|
| 1986 |
Nardo JV, Dawson JH. Spectroscopic evidence for the coordination of oxygen donor ligands to tetraphenylporphinatozinc Inorganica Chimica Acta. 123: 9-13. DOI: 10.1016/S0020-1693(00)81308-0 |
0.385 |
|
| 1985 |
Sono M, Eble KS, Dawson JH, Hager LP. Preparation and properties of ferrous chloroperoxidase complexes with dioxygen, nitric oxide, and an alkyl isocyanide. Spectroscopic dissimilarities between the oxygenated forms of chloroperoxidase and cytochrome P-450. The Journal of Biological Chemistry. 260: 15530-5. PMID 2999120 |
0.385 |
|
| 1985 |
Sono M, Dawson JH, Hager LP. Phosphine binding as a structural probe of the chloroperoxidase active site: Spectroscopic evidence for endogenous thiolate ligation to the heme iron Inorganic Chemistry. 24: 4339-4343. DOI: 10.1021/Ic00219A028 |
0.311 |
|
| 1985 |
Geno MJK, Dawson JH. Intramolecular electron transfer between osmium and cobalt centers bridged by a nonconjugated ligand [1] Inorganic Chemistry. 24: 1731-1732. DOI: 10.1002/Chin.198541308 |
0.339 |
|
| 1984 |
Eble KS, Dawson JH. NADH- and oxygen-dependent multiple turnovers of cytochrome P-450-CAM without putidaredoxin and putidaredoxin reductase. Biochemistry. 23: 2068-73. PMID 6722135 DOI: 10.1021/Bi00304A029 |
0.361 |
|
| 1984 |
Sono M, Dawson JH, Hager LP. The generation of a hyperporphyrin spectrum upon thiol binding to ferric chloroperoxidase. Further evidence of endogenous thiolate ligation to the ferric enzyme. The Journal of Biological Chemistry. 259: 13209-16. PMID 6541651 |
0.377 |
|
| 1984 |
Andersson LA, Dawson JH. The influence of oxygen donor ligation on the spectroscopic properties of ferric cytochrome P-450: ester, ether and ketone co-ordination to the haem iron. Xenobiotica; the Fate of Foreign Compounds in Biological Systems. 14: 49-61. PMID 6326394 DOI: 10.3109/00498258409151398 |
0.392 |
|
| 1984 |
Sono M, Dawson JH. Extensive studies of the heme coordination structure of indoleamine 2,3-dioxygenase and of tryptophan binding with magnetic and natural circular dichroism and electron paramagnetic resonance spectroscopy. Biochimica Et Biophysica Acta. 789: 170-87. PMID 6089893 DOI: 10.1016/0167-4838(84)90202-4 |
0.437 |
|
| 1984 |
Dooley DM, Dawson JH. Bioinorganic applications of magnetic circular dichroism spectroscopy: Copper, rare-earth ions, cobalt and non-heme iron systems Coordination Chemistry Reviews. 60: 1-66. DOI: 10.1016/0010-8545(84)85061-4 |
0.316 |
|
| 1984 |
Geno MJK, Dawson JH. Observation of an intervalence charge-transfer band in a mixed-valence ruthenium dimer bridged by a nonconjugated nitrogen donor ligand [2] Inorganic Chemistry. 23: 1182-1183. DOI: 10.1002/Chin.198430283 |
0.303 |
|
| 1983 |
Dawson JH, Andersson LA, Sono M. The diverse spectroscopic properties of ferrous cytochrome P-450-CAM ligand complexes. The Journal of Biological Chemistry. 258: 13637-45. PMID 6643443 |
0.318 |
|
| 1983 |
Andersson LA, Sono M, Dawson JH. Circular dichroism studies of low-spin ferric cytochrome P-450CAM ligand complexes. Biochimica Et Biophysica Acta. 748: 341-52. PMID 6639949 DOI: 10.1016/0167-4838(83)90178-4 |
0.436 |
|
| 1983 |
Dawson JH, Sono M, Hager LP. The active sites of chloroperoxidase and cytochrome P-450-CAM: Comparative spectroscopic and ligand binding properties Inorganica Chimica Acta. 79: 184-186. DOI: 10.1016/S0020-1693(00)95217-4 |
0.448 |
|
| 1982 |
Sono M, Andersson LA, Dawson JH. Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigation of the complexes. The Journal of Biological Chemistry. 257: 8308-20. PMID 6282878 |
0.356 |
|
| 1982 |
Dawson JH, Andersson LA, Sono M. Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme. The Journal of Biological Chemistry. 257: 3606-17. PMID 6277939 |
0.355 |
|
| 1981 |
Dooley DM, Dawson JH, Stephens PJ, Gray HB. Spectroscopic studies of ascorbate oxidase. Electronic structure of the blue copper sites. Biochemistry. 20: 2024-8. PMID 7225370 DOI: 10.1021/Bi00510A044 |
0.459 |
|
| 1981 |
Collman JP, Basolo F, Bunnenberg E, Collins TJ, Dawson JH, Ellis PE, Marrocco ML, Moscowitz A, Sessler JL, Szymanski T. Use of magnetic circular dichroism to determine axial ligation for some sterically encumbered iron(II) porphyrin complexes Journal of the American Chemical Society. 103: 5636-5648. DOI: 10.1021/Ja00409A003 |
0.523 |
|
| 1980 |
Dawson JH, Dooley DM, Gray HB. Coordination environment and fluoride binding of type 2 copper in the blue copper protein ascorbate oxidase. Proceedings of the National Academy of Sciences of the United States of America. 77: 5028-31. PMID 16592868 DOI: 10.1073/Pnas.77.9.5028 |
0.509 |
|
| 1980 |
Solomon EI, Hare JW, Dooley DM, Dawson JH, Stephens PJ, Gray HB. Spectroscopic studies of stellacyanin, plastocyanin, and azurin. Electronic structure of the blue copper sites Journal of the American Chemical Society. 102: 168-178. DOI: 10.1021/Ja00521A029 |
0.551 |
|
| 1979 |
Dawson JH, Dooley DM, Clark R, Stephens PJ, Gray HB. Spectroscopic studies of ceruloplasmin. Electronic structures of the copper sites Journal of the American Chemical Society. 101: 5046-5053. DOI: 10.1021/Ja00511A040 |
0.44 |
|
| 1979 |
Dooley DM, Rawlings J, Dawson JH, Stephens PJ, Andreasson L, Malmstrom BG, Gray HB. Spectroscopic studies of Rhus vernicifera and Polyporus versicolor laccase. Electronic structures of the copper sites Journal of the American Chemical Society. 101: 5038-5046. DOI: 10.1021/Ja00511A039 |
0.442 |
|
| 1978 |
Dawson JH, Cramer SP. Oxygenated cytochrome P-450cam: evidence against axial histidine ligation of iron. Febs Letters. 88: 127-30. PMID 639980 DOI: 10.1016/0014-5793(78)80623-1 |
0.577 |
|
| 1978 |
Dawson JH, Trudell JR, Linder RE, Barth G, Bunnenberg E, Djerassi C. Magnetic circular dichroism of purified forms of rabbit liver cytochromes P-450 and P-420. Biochemistry. 17: 33-42. PMID 618545 DOI: 10.1021/Bi00594A006 |
0.402 |
|
| 1978 |
Dawson JH, Dooley DM, Gray HB. Coordination environment and fluoride binding of type 2 copper in the blue copper oxidase ceruloplasmin. Proceedings of the National Academy of Sciences of the United States of America. 75: 4078-81. PMID 212731 DOI: 10.1073/Pnas.75.9.4078 |
0.491 |
|
| 1978 |
Cramer SP, Dawson JH, Hodgson KO, Hager LP. Studies of the ferric forms of cytochrome P-450 and chloroperoxidase by extended x-ray absotption fine structure. Characterization of the iron-nitrogen and iron-sulfur distances Journal of the American Chemical Society. 100: 7282-7290. DOI: 10.1021/Ja00491A027 |
0.57 |
|
| 1977 |
Dawson JH, Trudell JR, Barth G, Linder RE, Bunnenberg E, Djerassi C, Gouterman M, Connell CR, Sayer P. Magnetic circular dichroism studies of non-iron "hyper" porphyrin complexes as models for reduced + CO cytochrome P-450. Journal of the American Chemical Society. 99: 641-2. PMID 830697 DOI: 10.1021/Ja00444A070 |
0.484 |
|
| 1977 |
DAWSON JH, TRUDELL JR, BARTH G, LINDER RE, BUNNENBERG E, DJERASSI C, GOUTERMAN M, CONNELL CR, SAYER P. ChemInform Abstract: MAGNETIC CIRCULAR DICHROISM STUDIES. 51. MAGNETIC CIRCULAR DICHROISM STUDIES OF NON-IRON ′HYPER′ PORPHYRIN COMPLEXES AS MODELS FOR REDUCED + CARBON MONOXIDE CYTOCHROME P-450 Chemischer Informationsdienst. 8: no-no. DOI: 10.1002/Chin.197716043 |
0.454 |
|
| 1976 |
Dawson JH, Trudell JR, Barth G, Linder RE, Bunnenberg E, Djerassi C, Chiang R, Hager LP. Letter: Chloroperoxidase. Evidence for P-450 type heme environment from magnetic circular dichroism spectroscopy. Journal of the American Chemical Society. 98: 3709-10. PMID 1270707 DOI: 10.1021/Ja00428A055 |
0.432 |
|
| 1976 |
Dawson JH, Holm RH, Trudell JR, Barth G, Linder RE, Bunnenberg E, Djerassi C, Tang SC. Letter: Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism. Journal of the American Chemical Society. 98: 3707-8. PMID 1270706 DOI: 10.1021/Ja00428A054 |
0.484 |
|
| 1976 |
Collman JP, Sorrell TN, Dawson JH, Trudell JR, Bunnenberg E, Djerassi C. Magnetic circular dichroism of ferrous carbonyl adducts of cytochromes P-450 and P-420 and their synthetic models: further evidence for mercaptide as the fifth ligand to iron. Proceedings of the National Academy of Sciences of the United States of America. 73: 6-10. PMID 1061127 DOI: 10.1073/Pnas.73.1.6 |
0.534 |
|
| 1974 |
Dawson JH, Dolinger PM, Trudell JR, Barth G, Linder RE, Bunnenberg E, Djerassi C. Magnetic circular dichroism studies XXXV. A comparison of cytochromes P-450 and P-448. Proceedings of the National Academy of Sciences of the United States of America. 71: 4594-7. PMID 4531003 DOI: 10.1073/Pnas.71.11.4594 |
0.424 |
|
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