| Year |
Citation |
Score |
| 2022 |
Transue WJ, Snyder RA, Caranto JD, Kurtz DM, Solomon EI. Particle Swarm Fitting of Spin Hamiltonians: Magnetic Circular Dichroism of Reduced and NO-Bound Flavodiiron Protein. Inorganic Chemistry. PMID 36223761 DOI: 10.1021/acs.inorgchem.2c02234 |
0.71 |
|
| 2020 |
Benavides BS, Valandro S, Cioloboc D, Taylor AB, Schanze KS, Kurtz DM. Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. PMID 32283930 DOI: 10.1021/Acs.Biochem.9B01103 |
0.512 |
|
| 2020 |
Cioloboc D, Kurtz DM. Targeted cancer cell delivery of arsenate as a reductively activated prodrug. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 32189144 DOI: 10.1007/S00775-020-01774-3 |
0.315 |
|
| 2020 |
Benavides BS, Valandro S, Kurtz DM. Preparation of platinum nanoparticles using iron(II) as reductant and photosensitized H2 generation on an iron storage protein scaffold Rsc Advances. 10: 5551-5559. DOI: 10.1039/D0Ra00341G |
0.362 |
|
| 2020 |
Biswas S, Kurtz DM, Montoya SR, Hendrich MP, Bominaar EL. The Catalytic Role of a Conserved Tyrosine in Nitric Oxide Reducing Non-heme Diiron Enzymes Acs Catalysis. 10: 8177-8186. DOI: 10.1021/Acscatal.0C01884 |
0.411 |
|
| 2019 |
Benavides BS, Acharya R, Clark ER, Basak P, Maroney MJ, Nocek JM, Schanze KS, Kurtz DM. Structural, Photophysical, and Photochemical Characterization of Zinc Protoporphyrin IX in a Dimeric Variant of an Iron Storage Protein: Insights into the Mechanism of Photosensitized H Generation. The Journal of Physical Chemistry. B. PMID 31294990 DOI: 10.1021/Acs.Jpcb.9B04817 |
0.446 |
|
| 2018 |
Weitz AC, Giri N, Frederick RE, Kurtz DM, Bominaar EL, Hendrich MP. Spectroscopy and DFT Calculations of Flavo-Diiron Nitric Oxide Reductase Identify Bridging Structures of NO-Coordinated Diiron Intermediates. Acs Catalysis. 8: 11704-11715. PMID 31263628 DOI: 10.1021/Acscatal.8B03051 |
0.502 |
|
| 2017 |
Cioloboc D, Kennedy C, Boice EN, Clark ER, Kurtz DM. Trojan Horse for Light-Triggered Bifurcated Production of Singlet Oxygen and Fenton-Reactive Iron within Cancer Cells. Biomacromolecules. PMID 29192767 DOI: 10.1021/Acs.Biomac.7B01433 |
0.395 |
|
| 2017 |
Weitz AC, Giri N, Caranto JD, Kurtz DM, Bominaar EL, Hendrich MP. Spectroscopy and DFT calculations of a flavo-diiron enzyme implicate new diiron site structures. Journal of the American Chemical Society. PMID 28756660 DOI: 10.1021/Jacs.7B06546 |
0.761 |
|
| 2017 |
Clark ER, Kurtz DM. Photosensitized H2 Production Using a Zinc Porphyrin-Substituted Protein, Platinum Nanoparticles, and Ascorbate with No Electron Relay: Participation of Good's Buffers. Inorganic Chemistry. PMID 28362081 DOI: 10.1021/Acs.Inorgchem.7B00228 |
0.304 |
|
| 2016 |
Arkosi M, Scurtu F, Vulpoi A, Silaghi-Dumitrescu R, Kurtz D. Copolymerization of recombinant Phascolopsis gouldii hemerythrin with human serum albumin for use in blood substitutes. Artificial Cells, Nanomedicine, and Biotechnology. 45: 218-223. PMID 28034322 DOI: 10.1080/21691401.2016.1269118 |
0.304 |
|
| 2016 |
Miner KD, Kurtz DM. Active Site Metal Occupancy and Cyclic di-GMP Phosphodiesterase Activity of Thermotoga maritima HD-GYP. Biochemistry. PMID 26786892 DOI: 10.1021/Acs.Biochem.5B01227 |
0.401 |
|
| 2015 |
Clark ER, Kurtz DM. Photosensitized H2 generation from "one-pot" and "two-pot" assemblies of a zinc-porphyrin/platinum nanoparticle/protein scaffold. Dalton Transactions (Cambridge, England : 2003). PMID 26616549 DOI: 10.1039/C5Dt03418C |
0.343 |
|
| 2015 |
Kwak Y, Schwartz JK, Huang VW, Boice E, Kurtz DM, Solomon EI. CD/MCD/VTVH-MCD Studies of Escherichia coli Bacterioferritin Support a Binuclear Iron Cofactor Site. Biochemistry. PMID 26551523 DOI: 10.1021/Acs.Biochem.5B01033 |
0.511 |
|
| 2015 |
Frederick RE, Caranto JD, Masitas CA, Gebhardt LL, MacGowan CE, Limberger RJ, Kurtz DM. Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysis. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 20: 603-13. PMID 25700637 DOI: 10.1007/S00775-015-1248-4 |
0.755 |
|
| 2015 |
Boice E, Kurtz D. A Trojan Horse for Light-Triggered Delivery of Toxic Iron to Cancer Cells The Faseb Journal. 29. DOI: 10.1096/Fasebj.29.1_Supplement.897.20 |
0.302 |
|
| 2014 |
Caranto JD, Weitz A, Giri N, Hendrich MP, Kurtz DM. A diferrous-dinitrosyl intermediate in the N2O-generating pathway of a deflavinated flavo-diiron protein. Biochemistry. 53: 5631-7. PMID 25144650 DOI: 10.1021/Bi500836Z |
0.756 |
|
| 2014 |
Miriani M, Iametti S, Kurtz DM, Bonomi F. Rubredoxin refolding on nanostructured hydrophobic surfaces: evidence for a new type of biomimetic chaperones. Proteins. 82: 3154-62. PMID 25143010 DOI: 10.1002/Prot.24675 |
0.312 |
|
| 2014 |
Caranto JD, Weitz A, Hendrich MP, Kurtz DM. The nitric oxide reductase mechanism of a flavo-diiron protein: identification of active-site intermediates and products. Journal of the American Chemical Society. 136: 7981-92. PMID 24828196 DOI: 10.1021/Ja5022443 |
0.78 |
|
| 2014 |
Hathazi D, Mot AC, Vaida A, Scurtu F, Lupan I, Fischer-Fodor E, Damian G, Kurtz DM, Silaghi-Dumitrescu R. Oxidative protection of hemoglobin and hemerythrin by cross-linking with a nonheme iron peroxidase: potentially improved oxygen carriers for use in blood substitutes. Biomacromolecules. 15: 1920-7. PMID 24716617 DOI: 10.1021/Bm5004256 |
0.443 |
|
| 2014 |
Okamoto Y, Onoda A, Sugimoto H, Takano Y, Hirota S, Kurtz DM, Shiro Y, Hayashi T. H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin. Chemical Communications (Cambridge, England). 50: 3421-3. PMID 24400317 DOI: 10.1039/C3Cc48108E |
0.413 |
|
| 2014 |
Opel-Reading H, Luckner S, Schaller R, Kurtz D, Krause K. Rubrerythrin from Trichomonas vaginalis- structural insights into its mechanism of action Acta Crystallographica Section a Foundations and Advances. 70: C821-C821. DOI: 10.1107/S2053273314091785 |
0.427 |
|
| 2013 |
Okamoto Y, Onoda A, Sugimoto H, Takano Y, Hirota S, Kurtz DM, Shiro Y, Hayashi T. Crystal structure, exogenous ligand binding, and redox properties of an engineered diiron active site in a bacterial hemerythrin. Inorganic Chemistry. 52: 13014-20. PMID 24187962 DOI: 10.1021/Ic401632X |
0.405 |
|
| 2013 |
Miner KD, Klose KE, Kurtz DM. An HD-GYP cyclic di-guanosine monophosphate phosphodiesterase with a non-heme diiron-carboxylate active site. Biochemistry. 52: 5329-31. PMID 23883166 DOI: 10.1021/Bi4009215 |
0.378 |
|
| 2012 |
Schaller RA, Ali SK, Klose KE, Kurtz DM. A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase. Biochemistry. 51: 8563-70. PMID 23057727 DOI: 10.1021/Bi3011797 |
0.397 |
|
| 2012 |
Fang H, Caranto JD, Mendoza R, Taylor AB, Hart PJ, Kurtz DM. Histidine ligand variants of a flavo-diiron protein: effects on structure and activities. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 1231-9. PMID 22990880 DOI: 10.1007/S00775-012-0938-4 |
0.746 |
|
| 2012 |
Caranto JD, Gebhardt LL, MacGowan CE, Limberger RJ, Kurtz DM. Treponema denticola superoxide reductase: in vivo role, in vitro reactivities, and a novel [Fe(Cys)(4)] site. Biochemistry. 51: 5601-10. PMID 22715932 DOI: 10.1021/Bi300667S |
0.765 |
|
| 2012 |
Hayashi T, Caranto JD, Matsumura H, Kurtz DM, Moënne-Loccoz P. Vibrational analysis of mononitrosyl complexes in hemerythrin and flavodiiron proteins: relevance to detoxifying NO reductase. Journal of the American Chemical Society. 134: 6878-84. PMID 22449095 DOI: 10.1021/Ja301812P |
0.754 |
|
| 2010 |
Hayashi T, Caranto JD, Wampler DA, Kurtz DM, Moënne-Loccoz P. Insights into the nitric oxide reductase mechanism of flavodiiron proteins from a flavin-free enzyme. Biochemistry. 49: 7040-9. PMID 20669924 DOI: 10.1021/Bi100788Y |
0.767 |
|
| 2010 |
Morleo A, Bonomi F, Iametti S, Huang VW, Kurtz DM. Iron-nucleated folding of a metalloprotein in high urea: resolution of metal binding and protein folding events. Biochemistry. 49: 6627-34. PMID 20614892 DOI: 10.1021/Bi100630T |
0.471 |
|
| 2010 |
Mot AC, Roman A, Lupan I, Kurtz DM, Silaghi-Dumitrescu R. Towards the development of hemerythrin-based blood substitutes. The Protein Journal. 29: 387-93. PMID 20582620 DOI: 10.1007/S10930-010-9264-2 |
0.306 |
|
| 2009 |
Riebe O, Fischer RJ, Wampler DA, Kurtz DM, Bahl H. Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum. Microbiology (Reading, England). 155: 16-24. PMID 19118342 DOI: 10.1099/Mic.0.022756-0 |
0.403 |
|
| 2009 |
Hillmann F, Riebe O, Fischer RJ, Mot A, Caranto JD, Kurtz DM, Bahl H. Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum. Febs Letters. 583: 241-5. PMID 19084524 DOI: 10.1016/J.Febslet.2008.12.004 |
0.721 |
|
| 2008 |
Bonomi F, Iametti S, Ferranti P, Kurtz DM, Morleo A, Ragg EM. "Iron priming" guides folding of denatured aporubredoxins. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 981-91. PMID 18446387 DOI: 10.1007/S00775-008-0385-4 |
0.475 |
|
| 2007 |
Huang VW, Emerson JP, Kurtz DM. Reaction of Desulfovibrio vulgaris two-iron superoxide reductase with superoxide: insights from stopped-flow spectrophotometry. Biochemistry. 46: 11342-51. PMID 17854204 DOI: 10.1021/Bi700450U |
0.65 |
|
| 2007 |
Kurtz DM. Flavo-diiron enzymes: Nitric oxide or dioxygen reductases? Dalton Transactions. 4115-4121. DOI: 10.1039/B710047G |
0.412 |
|
| 2006 |
Yang TC, McNaughton RL, Clay MD, Jenney FE, Krishnan R, Kurtz DM, Adams MW, Johnson MK, Hoffman BM. Comparing the electronic properties of the low-spin cyano-ferric [Fe(N4)(Cys)] active sites of superoxide reductase and p450cam using ENDOR spectroscopy and DFT calculations. Journal of the American Chemical Society. 128: 16566-78. PMID 17177406 DOI: 10.1021/Ja064656P |
0.442 |
|
| 2006 |
Isaza CE, Silaghi-Dumitrescu R, Iyer RB, Kurtz DM, Chan MK. Structural basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: substrate tunnel and fluxional N terminus. Biochemistry. 45: 9023-31. PMID 16866347 DOI: 10.1021/Bi0607812 |
0.362 |
|
| 2006 |
Kurtz DM. Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin. Journal of Inorganic Biochemistry. 100: 679-93. PMID 16504301 DOI: 10.1016/j.jinorgbio.2005.12.017 |
0.411 |
|
| 2006 |
Clay MD, Yang TC, Jenney FE, Kung IY, Cosper CA, Krishnan R, Kurtz DM, Adams MW, Hoffman BM, Johnson MK. Geometries and electronic structures of cyanide adducts of the non-heme iron active site of superoxide reductases: vibrational and ENDOR studies. Biochemistry. 45: 427-38. PMID 16401073 DOI: 10.1021/Bi052034V |
0.378 |
|
| 2005 |
Iyer RB, Silaghi-Dumitrescu R, Kurtz DM, Lanzilotta WN. High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 407-16. PMID 15895271 DOI: 10.1007/s00775-005-0650-8 |
0.398 |
|
| 2005 |
Silaghi-Dumitrescu R, Kurtz DM, Ljungdahl LG, Lanzilotta WN. X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase. Biochemistry. 44: 6492-501. PMID 15850383 DOI: 10.1021/Bi0473049 |
0.401 |
|
| 2004 |
Kurtz DM. Microbial detoxification of superoxide: the non-heme iron reductive paradigm for combating oxidative stress. Accounts of Chemical Research. 37: 902-8. PMID 15612680 DOI: 10.1021/ar0200091 |
0.416 |
|
| 2004 |
Jin S, Kurtz DM, Liu ZJ, Rose J, Wang BC. Displacement of iron by zinc at the diiron site of Desulfovibrio vulgaris rubrerythrin: X-ray crystal structure and anomalous scattering analysis. Journal of Inorganic Biochemistry. 98: 786-96. PMID 15134924 DOI: 10.1016/j.jinorgbio.2004.01.005 |
0.335 |
|
| 2004 |
Jin S, Kurtz DM, Liu ZJ, Rose J, Wang BC. X-ray crystal structure of Desulfovibrio vulgaris rubrerythrin with zinc substituted into the [Fe(SCys)4] site and alternative diiron site structures. Biochemistry. 43: 3204-13. PMID 15023070 DOI: 10.1021/bi0356193 |
0.387 |
|
| 2004 |
Bonomi F, Eidsness MK, Iametti S, Kurtz DM, Mazzini S, Morleo A. Contribution of the [FeII(SCys)4] site to the thermostability of rubredoxins. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 297-306. PMID 14770302 DOI: 10.1007/s00775-004-0525-4 |
0.383 |
|
| 2004 |
Kurtz DM, Coulter ED. Bacterial nonheme iron proteins and oxidative stress Chemtracts. 17: 127-155. |
0.314 |
|
| 2003 |
Beharry ZM, Eby DM, Coulter ED, Viswanathan R, Neidle EL, Phillips RS, Kurtz DM. Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase. Biochemistry. 42: 13625-36. PMID 14622009 DOI: 10.1021/Bi035385N |
0.455 |
|
| 2003 |
Emerson JP, Coulter ED, Phillips RS, Kurtz DM. Kinetics of the superoxide reductase catalytic cycle. The Journal of Biological Chemistry. 278: 39662-8. PMID 12900405 DOI: 10.1074/Jbc.M306488200 |
0.635 |
|
| 2003 |
Clay MD, Emerson JP, Coulter ED, Kurtz DM, Johnson MK. Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 671-82. PMID 12764688 DOI: 10.1007/S00775-003-0465-4 |
0.632 |
|
| 2003 |
Smoukov SK, Davydov RM, Doan PE, Sturgeon B, Kung IY, Hoffman BM, Kurtz DM. EPR and ENDOR evidence for a 1-His, hydroxo-bridged mixed-valent diiron site in Desulfovibrio vulgaris rubrerythrin. Biochemistry. 42: 6201-8. PMID 12755623 DOI: 10.1021/Bi0300027 |
0.396 |
|
| 2003 |
Silaghi-Dumitrescu R, Silaghi-Dumitrescu I, Coulter ED, Kurtz DM. Computational study of the non-heme iron active site in superoxide reductase and its reaction with superoxide. Inorganic Chemistry. 42: 446-56. PMID 12693226 DOI: 10.1021/ic025684l |
0.422 |
|
| 2003 |
Emerson JP, Cabelli DE, Kurtz DM. An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo. Proceedings of the National Academy of Sciences of the United States of America. 100: 3802-7. PMID 12637682 DOI: 10.1073/Pnas.0537177100 |
0.644 |
|
| 2003 |
Silaghi-Dumitrescu R, Coulter ED, Das A, Ljungdahl LG, Jameson GN, Huynh BH, Kurtz DM. A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity. Biochemistry. 42: 2806-15. PMID 12627946 DOI: 10.1021/Bi027253K |
0.411 |
|
| 2003 |
Kurtz DM, Silaghi-Dumitrescu R, Das A, Jameson GN, Ljungdahl LG, Huynh BH. A non-theme iron nitric oxide reductase that protects against nitrosative stress in acetogenic bacteria Journal of Inorganic Biochemistry. 96: 174. DOI: 10.1016/S0162-0134(03)80682-7 |
0.411 |
|
| 2003 |
Kurtz DM, Emerson JP, Silaghi-Dumitrescu R, Kung I, Das A, Ljungdahl LG. How microbes detoxify superoxide, hydrogen peroxide and nitric oxide. The non-heme iron reductive paradigm Journal of Inorganic Biochemistry. 96: 69. DOI: 10.1016/S0162-0134(03)80519-6 |
0.652 |
|
| 2002 |
Jin S, Kurtz DM, Liu ZJ, Rose J, Wang BC. X-ray crystal structures of reduced rubrerythrin and its azide adduct: a structure-based mechanism for a non-heme diiron peroxidase. Journal of the American Chemical Society. 124: 9845-55. PMID 12175244 DOI: 10.1021/ja026587u |
0.373 |
|
| 2002 |
Kurtz DM, Coulter ED. The mechanism(s) of superoxide reduction by superoxide reductases in vitro and in vivo. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 653-8. PMID 12072973 DOI: 10.1007/s00775-002-0360-4 |
0.349 |
|
| 2002 |
Bonomi F, Burden AE, Eidsness MK, Fessas D, Iametti S, Kurtz DM, Mazzini S, Scott RA, Zeng Q. Thermal stability of the [Fe(SCys)(4)] site in Clostridium pasteurianum rubredoxin: contributions of the local environment and Cys ligand protonation. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 427-36. PMID 11941500 DOI: 10.1007/s00775-001-0314-2 |
0.361 |
|
| 2002 |
Emerson JP, Coulter ED, Cabelli DE, Phillips RS, Kurtz DM. Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris. Biochemistry. 41: 4348-57. PMID 11914081 DOI: 10.1021/Bi0119159 |
0.65 |
|
| 2001 |
Coulter ED, Kurtz DM. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Archives of Biochemistry and Biophysics. 394: 76-86. PMID 11566030 DOI: 10.1006/abbi.2001.2531 |
0.311 |
|
| 2001 |
Eby DM, Beharry ZM, Coulter ED, Kurtz DM, Neidle EL. Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1. Journal of Bacteriology. 183: 109-18. PMID 11114907 DOI: 10.1128/JB.183-1.109-118.2001 |
0.303 |
|
| 1999 |
Kurtz DM. Oxygen-carrying proteins: three solutions to a common problem. Essays in Biochemistry. 34: 85-100. PMID 10730190 |
0.31 |
|
| 1999 |
Coulter ED, Shenvi NV, Kurtz DM. NADH peroxidase activity of rubrerythrin. Biochemical and Biophysical Research Communications. 255: 317-23. PMID 10049706 DOI: 10.1006/bbrc.1999.0197 |
0.335 |
|
| 1996 |
Garg RP, Vargo CJ, Cui X, Kurtz DM. A [2Fe-2S] protein encoded by an open reading frame upstream of the Escherichia coli bacterioferritin gene. Biochemistry. 35: 6297-301. PMID 8639572 DOI: 10.1021/bi9600862 |
0.33 |
|
| 1995 |
Gupta N, Bonomi F, Kurtz DM, Ravi N, Wang DL, Huynh BH. Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain. Biochemistry. 34: 3310-8. PMID 7880826 |
0.363 |
|
| 1994 |
Klotz IM, Kurtz DM. Metal-Dioxygen Complexes: A Perspective Chemical Reviews. 94: 567-568. DOI: 10.1021/Cr00027A001 |
0.388 |
|
| 1993 |
Ravi N, Prickril BC, Kurtz DM, Huynh BH. Spectroscopic characterization of 57Fe-reconstituted rubrerythrin, a non-heme iron protein with structural analogies to ribonucleotide reductase. Biochemistry. 32: 8487-91. PMID 8395205 |
0.343 |
|
| 1993 |
Prickril BC, Kurtz DM, Gupta N, Ravi N, Huynh B, Bonomi F. Rubrerythrin: A non-heme iron protein with structural analogies to ribonucleotide reductase. Journal of Inorganic Biochemistry. 51: 508. DOI: 10.1016/0162-0134(93)85536-H |
0.425 |
|
| 1992 |
Zhang JH, Kurtz DM, Xia YM, Debrunner PG. Conversion of non-functional to functional iron following reconstitution of hemerythrin. Biochimica Et Biophysica Acta. 1122: 293-8. PMID 1504090 DOI: 10.1016/0167-4838(92)90407-5 |
0.371 |
|
| 1992 |
Zhang JH, Kurtz DM, Maroney MJ, Whitehead JP. Metal substitutions at the diiron site of hemerythrin. A dicobalt(II) derivative Inorganic Chemistry. 31: 1359-1366. DOI: 10.1021/Ic00034A013 |
0.361 |
|
| 1991 |
Zhang JH, Kurtz DM, Xia YM, Debrunner PG. Reconstitution of the diiron sites in hemerythrin and myohemerythrin. Biochemistry. 30: 583-9. PMID 1988045 DOI: 10.1021/Bi00216A037 |
0.391 |
|
| 1989 |
Kurtz D, Bonomi F, Iametti S. Acceleration of the synthesis of thiomolybdate from molybdate and sodium sulfide by thiols and iron Journal of Inorganic Biochemistry. 36: 179. DOI: 10.1016/0162-0134(89)84104-2 |
0.382 |
|
| 1989 |
Werth MT, Kurtz DM, Howes BD, Huynh BH. Observation of S = 2 EPR signals from ferrous iron-thiolate complexes. Relevance to rubredoxin-type sites in proteins Inorganic Chemistry. 28: 1357-1361. |
0.318 |
|
| 1988 |
Nocek JM, Kurtz DM, Sage JT, Xia YM, Debrunner P, Shiemke AK, Sanders-Loehr J, Loehr TM. Nitric oxide adducts of the binuclear iron site of hemerythrin: spectroscopy and reactivity. Biochemistry. 27: 1014-24. PMID 3365363 DOI: 10.1021/Bi00403A026 |
0.45 |
|
| 1988 |
Utecht RE, Kurtz DM. Cytochrome b5 and NADH-cytochrome-b5 reductase from sipunculan erythrocytes; a methemerythrin reduction system from Phascolopsis gouldii. Biochimica Et Biophysica Acta. 953: 164-78. PMID 2831990 DOI: 10.1016/0167-4838(88)90021-0 |
0.31 |
|
| 1987 |
Pearce LL, Utecht RE, Kurtz DM. Comparisons of redox kinetics of methemerythrin and mu-sulfidomethemerythrin. Implications for interactions with cytochrome b5. Biochemistry. 26: 8709-17. PMID 2831950 |
0.365 |
|
| 1986 |
Maroney MJ, Kurtz DM, Nocek JM, Pearce LL, Que L. 1H NMR probes of the binuclear iron cluster in hemerythrin Journal of the American Chemical Society. 108: 6871-6879. DOI: 10.1021/Ja00282A005 |
0.333 |
|
| 1985 |
Bonomi F, Pagani S, Kurtz DM. Enzymic synthesis of the 4Fe-4S clusters of Clostridium pasteurianum ferredoxin. European Journal of Biochemistry / Febs. 148: 67-73. PMID 2983992 DOI: 10.1111/J.1432-1033.1985.Tb08808.X |
0.435 |
|
| 1985 |
Nocek JM, Kurtz DM, Sage JT, Debrunner PG, Maroney MJ, Que L. Nitric oxide adduct of the binuclear iron center in deoxyhemerythrin from Phascolopsis gouldii. Analogue of a putative intermediate in the oxygenation reaction Journal of the American Chemical Society. 107: 3382-3384. DOI: 10.1021/Ja00297A074 |
0.443 |
|
| 1985 |
Bonomi F, Werth MT, Kurtz DM. Assembly of [FenSn(SR)4]2- (n = 2, 4) in aqueous media from iron salts, thiols, and sulfur, sulfide, or thiosulfate plus rhodanese Inorganic Chemistry. 24: 4331-4335. DOI: 10.1021/Ic00219A026 |
0.389 |
|
| 1985 |
Stevens WC, Kurtz DM. Assembly of [FenSn(SPh)4]2- (n = 2, 4) and their iron-thiolate precursors in aqueous media Inorganic Chemistry. 24: 3444-3449. DOI: 10.1021/Ic00215A029 |
0.344 |
|
| 1985 |
Lukat GS, Kurtz DM. Redox chemistry of sulfide-bridged derivatives of the binuclear iron site in hemerythrin from Phascolopsis gouldii Biochemistry. 24: 3464-3472. DOI: 10.1021/Bi00335A012 |
0.446 |
|
| 1984 |
Lukat GS, Kurtz DM, Shiemke AK, Loehr TM, Sanders-Loehr J. Sulfide-bridged derivatives of the binuclear iron site of hemerythrin at both met and semi-met oxidation levels. Biochemistry. 23: 6416-22. PMID 6529557 DOI: 10.1021/Bi00321A021 |
0.492 |
|
| 1984 |
Bonomi F, Kurtz DM. Chromatographic separation of extruded iron-sulfur cores from the apoproteins of Clostridium pasteurianum and spinach ferredoxins in aqueous Triton X-100/urea. Analytical Biochemistry. 142: 226-31. PMID 6517316 DOI: 10.1016/0003-2697(84)90543-8 |
0.438 |
|
| 1984 |
Klotz IM, Kurtz DM. Binuclear oxygen carriers: Hemerythrin Accounts of Chemical Research. 17: 16-22. DOI: 10.1021/Ar00097A003 |
0.465 |
|
| 1984 |
Kurtz DM, Stevens WC. Assembly of the iron-sulfur cluster [FenSn(SPh)4]2- (n = 2, 4) in aqueous-based media Journal of the American Chemical Society. 106: 1523-1524. DOI: 10.1002/Chin.198425264 |
0.348 |
|
| 1983 |
Kurtz DM, Sage JT, Hendrich M, Debrunner PG, Lukat GS. Semi-met oxidation level of chalcogenide derivatives of methemerythrin. Mössbauer and EPR studies. The Journal of Biological Chemistry. 258: 2115-7. PMID 6296130 |
0.382 |
|
| 1983 |
Kurtz DM. Core extrusion of the two [4Fe4S] centers of C. pasteurianum ferredoxin in aqueous triton Inorganica Chimica Acta. 80: L75-L76. DOI: 10.1016/S0020-1693(00)91252-0 |
0.378 |
|
| 1982 |
Bonomi F, Kurtz DM. Kinetics and equilibria of active site core extrusion from spinach ferredoxin in aqueous N,N-dimethylformamide/Triton X-100 solutions. Biochemistry. 21: 6838-43. PMID 7159566 DOI: 10.1021/Bi00269A033 |
0.313 |
|
| 1982 |
Kurtz DM. A new method for extrusion of iron-sulfur cores from active centers of proteins. Biochemical and Biophysical Research Communications. 104: 437-42. PMID 7073692 DOI: 10.1016/0006-291X(82)90656-8 |
0.442 |
|
| 1979 |
Kurtz DM, Holm RH, Ruzicka FJ, Beinert H, Coles CJ, Singer TP. The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster. The Journal of Biological Chemistry. 254: 4967-9. PMID 447628 |
0.302 |
|
| 1979 |
Kurtz DM, McMillan RS, Burgess BK, Mortenson LE, Holm RH. Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase. Proceedings of the National Academy of Sciences of the United States of America. 76: 4986-9. PMID 291915 DOI: 10.1073/Pnas.76.10.4986 |
0.346 |
|
| 1979 |
Coles CJ, Holm RH, Kurtz DM, Orme-Johnson WH, Rawlings J, Singer TP, Wong GB. Characterization of the iron-sulfur centers in succinate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 76: 3805-8. PMID 226982 DOI: 10.1073/Pnas.76.8.3805 |
0.346 |
|
| 1976 |
Kurtz DM, Shriver DF, Klotz IM. Letter: Resonance raman spectroscopy with unsymmetrically isotopic ligands. Differentiation of possible structures of hemerythrin complexes. Journal of the American Chemical Society. 98: 5033-5. PMID 950426 DOI: 10.1021/Ja00432A064 |
0.484 |
|
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