RCMI Coordinating Center (RCMI CC) Header Logo

Donald Kurtz

TitleProfessor
InstitutionUniversity of Texas at San Antonio
Departmentchemistry
Address1 UTSA Cir
San Antonio TX 78249
Phone(210) 458-7060
vCardDownload vCard

    Collapse Overview 
    Collapse overview
    A major aspect of our research focuses on the structure, function, and catalytic mechanisms of bacterial and archaeal non-heme iron enzymes that reductively scavenge diatomic oxygen and nitrogen species. These scavenging and sensing reactions require specialized active sites with novel iron coordination environments and novel mechanisms, which we follow by rapid kinetic and spectroscopic techniques as well as protein X-ray crystallography. We are also attempting to develop an oxygen-carrying protein as a blood substitute.
    A related project focuses on proteins that catalyze storage and release of intracellular iron. An exciting new development is the use of these iron storage proteins as scaffolds to enclose metal and semiconductor nanoparticles for photochemical H2 production and photo-initiated delivery of toxic iron to cancer cells.


    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
    Newest   |   Oldest   |   Most Cited   |   Most Discussed   |   Timeline   |   Field Summary   |   Plain Text
    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. 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. 2020 Apr 28; 59(16):1618-1629. PMID: 32283930.
      Citations:    Fields:    
    2. Cioloboc D, Kurtz DM. Targeted cancer cell delivery of arsenate as a reductively activated prodrug. J Biol Inorg Chem. 2020 May; 25(3):441-449. PMID: 32189144.
      Citations:    Fields:    
    3. 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 H2 Generation. J Phys Chem B. 2019 08 08; 123(31):6740-6749. PMID: 31294990.
      Citations:    Fields:    
    4. 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 Catal. 2018 Dec 07; 8(12):11704-11715. PMID: 31263628.
      Citations:    
    5. 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. 2018 01 08; 19(1):178-187. PMID: 29192767.
      Citations:    Fields:    Translation:HumansCells
    6. Aboumatar H, Naqibuddin M, Chung S, Adebowale H, Bone L, Brown T, Cooper LA, Gurses AP, Knowlton A, Kurtz D, Piet L, Putcha N, Rand C, Roter D, Shattuck E, Sylvester C, Urteaga-Fuentes A, Wise R, Wolff JL, Yang T, Hibbard J, Howell E, Myers M, Shea K, Sullivan J, Syron L, Wang NY, Pronovost P. Better Respiratory Education and Treatment Help Empower (BREATHE) study: Methodology and baseline characteristics of a randomized controlled trial testing a transitional care program to improve patient-centered care delivery among chronic obstructive pulmonary disease patients. Contemp Clin Trials. 2017 11; 62:159-167. PMID: 28887069.
      Citations: 2     Fields:    Translation:Humans
    7. 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. J Am Chem Soc. 2017 08 30; 139(34):12009-12019. PMID: 28756660.
      Citations: 1     Fields:    Translation:Cells
    8. 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. Inorg Chem. 2017 Apr 17; 56(8):4585-4594. PMID: 28362081.
      Citations:    Fields:    Translation:Cells
    9. 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. Artif Cells Nanomed Biotechnol. 2017 Mar; 45(2):218-223. PMID: 28034322.
      Citations: 2     Fields:    Translation:HumansAnimals
    10. Miner KD, Kurtz DM. Active Site Metal Occupancy and Cyclic Di-GMP Phosphodiesterase Activity of Thermotoga maritima HD-GYP. Biochemistry. 2016 Feb 16; 55(6):970-9. PMID: 26786892.
      Citations: 4     Fields:    Translation:AnimalsCells
    11. Clark ER, Kurtz DM. Photosensitized H2 generation from "one-pot" and "two-pot" assemblies of a zinc-porphyrin/platinum nanoparticle/protein scaffold. Dalton Trans. 2016 Jan 14; 45(2):630-8. PMID: 26616549.
      Citations: 1     Fields:    Translation:Cells
    12. 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. 2015 Dec 01; 54(47):7010-8. PMID: 26551523.
      Citations: 2     Fields:    Translation:Cells
    13. 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. J Biol Inorg Chem. 2015 Apr; 20(3):603-13. PMID: 25700637.
      Citations: 4     Fields:    Translation:Cells
    14. Miriani M, Iametti S, Kurtz DM, Bonomi F. Rubredoxin refolding on nanostructured hydrophobic surfaces: evidence for a new type of biomimetic chaperones. Proteins. 2014 Nov; 82(11):3154-62. PMID: 25143010.
      Citations:    Fields:    Translation:Cells
    15. 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. 2014 Sep 09; 53(35):5631-7. PMID: 25144650.
      Citations: 4     Fields:    Translation:Cells
    16. 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. J Am Chem Soc. 2014 Jun 04; 136(22):7981-92. PMID: 24828196.
      Citations: 8     Fields:    Translation:Cells
    17. 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. 2014 May 12; 15(5):1920-7. PMID: 24716617.
      Citations: 5     Fields:    Translation:HumansCells
    18. 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. Chem Commun (Camb). 2014 Apr 04; 50(26):3421-3. PMID: 24400317.
      Citations:    Fields:    Translation:Cells
    19. 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. Inorg Chem. 2013 Nov 18; 52(22):13014-20. PMID: 24187962.
      Citations: 4     Fields:    Translation:Cells
    20. Miner KD, Klose KE, Kurtz DM. An HD-GYP cyclic di-guanosine monophosphate phosphodiesterase with a non-heme diiron-carboxylate active site. Biochemistry. 2013 Aug 13; 52(32):5329-31. PMID: 23883166.
      Citations: 10     Fields:    Translation:Cells
    21. Schaller RA, Ali SK, Klose KE, Kurtz DM. A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase. Biochemistry. 2012 Oct 30; 51(43):8563-70. PMID: 23057727.
      Citations: 11     Fields:    Translation:Cells
    22. 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. J Biol Inorg Chem. 2012 Dec; 17(8):1231-9. PMID: 22990880.
      Citations: 13     Fields:    Translation:Cells
    23. 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. 2012 Jul 17; 51(28):5601-10. PMID: 22715932.
      Citations: 3     Fields:    Translation:Cells
    24. 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. J Am Chem Soc. 2012 Apr 18; 134(15):6878-84. PMID: 22449095.
      Citations: 11     Fields:    
    25. 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. 2010 Aug 24; 49(33):7040-9. PMID: 20669924.
      Citations: 17     Fields:    Translation:Cells
    26. 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. 2010 Aug 10; 49(31):6627-34. PMID: 20614892.
      Citations: 5     Fields:    Translation:Cells
    27. Mot AC, Roman A, Lupan I, Kurtz DM, Silaghi-Dumitrescu R. Towards the development of hemerythrin-based blood substitutes. Protein J. 2010 Aug; 29(6):387-93. PMID: 20582620.
      Citations: 3     Fields:    Translation:AnimalsCells
    28. Riebe O, Fischer RJ, Wampler DA, Kurtz DM, Bahl H. Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum. Microbiology. 2009 Jan; 155(Pt 1):16-24. PMID: 19118342.
      Citations: 26     Fields:    Translation:Cells
    29. 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 Lett. 2009 Jan 05; 583(1):241-5. PMID: 19084524.
      Citations: 15     Fields:    Translation:Cells
    30. Bonomi F, Iametti S, Ferranti P, Kurtz DM, Morleo A, Ragg EM. "Iron priming" guides folding of denatured aporubredoxins. J Biol Inorg Chem. 2008 Aug; 13(6):981-91. PMID: 18446387.
      Citations: 3     Fields:    Translation:Cells
    31. Huang VW, Emerson JP, Kurtz DM. Reaction of Desulfovibrio vulgaris two-iron superoxide reductase with superoxide: insights from stopped-flow spectrophotometry. Biochemistry. 2007 Oct 09; 46(40):11342-51. PMID: 17854204.
      Citations: 11     Fields:    Translation:Cells
    32. 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. J Am Chem Soc. 2006 Dec 27; 128(51):16566-78. PMID: 17177406.
      Citations: 3     Fields:    Translation:Cells
    33. 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. 2006 Aug 01; 45(30):9023-31. PMID: 16866347.
      Citations: 23     Fields:    Translation:Cells
    34. Mydel P, Takahashi Y, Yumoto H, Sztukowska M, Kubica M, Gibson FC, Kurtz DM, Travis J, Collins LV, Nguyen KA, Genco CA, Potempa J. Roles of the host oxidative immune response and bacterial antioxidant rubrerythrin during Porphyromonas gingivalis infection. PLoS Pathog. 2006 Jul; 2(7):e76. PMID: 16895445.
      Citations: 47     Fields:    Translation:HumansAnimalsCells
    35. Kurtz DM. Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin. J Inorg Biochem. 2006 Apr; 100(4):679-93. PMID: 16504301.
      Citations: 28     Fields:    Translation:Cells
    36. 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. 2006 Jan 17; 45(2):427-38. PMID: 16401073.
      Citations: 5     Fields:    Translation:Cells
    37. 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. J Biol Inorg Chem. 2005 Aug; 10(5):592. PMID: 27518783.
      Citations:    Fields:    
    38. 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. J Biol Inorg Chem. 2005 Jun; 10(4):407-16. PMID: 15895271.
      Citations: 11     Fields:    Translation:Cells
    39. 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. 2005 May 03; 44(17):6492-501. PMID: 15850383.
      Citations: 37     Fields:    Translation:Cells
    40. Silaghi-Dumitrescu R, Ng KY, Viswanathan R, Kurtz DM. A flavo-diiron protein from Desulfovibrio vulgaris with oxidase and nitric oxide reductase activities. Evidence for an in vivo nitric oxide scavenging function. Biochemistry. 2005 Mar 08; 44(9):3572-9. PMID: 15736966.
      Citations: 25     Fields:    Translation:Cells
    41. Das A, Silaghi-Dumitrescu R, Ljungdahl LG, Kurtz DM. Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica. J Bacteriol. 2005 Mar; 187(6):2020-9. PMID: 15743950.
      Citations: 30     Fields:    Translation:Cells
    42. Kurtz DM. Microbial detoxification of superoxide: the non-heme iron reductive paradigm for combating oxidative stress. Acc Chem Res. 2004 Nov; 37(11):902-8. PMID: 15612680.
      Citations: 25     Fields:    Translation:Cells
    43. 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. J Inorg Biochem. 2004 May; 98(5):786-96. PMID: 15134924.
      Citations: 6     Fields:    Translation:Cells
    44. 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. 2004 Mar 23; 43(11):3204-13. PMID: 15023070.
      Citations: 6     Fields:    Translation:Cells
    45. Bonomi F, Eidsness MK, Iametti S, Kurtz DM, Mazzini S, Morleo A. Contribution of the [FeII(SCys)4] site to the thermostability of rubredoxins. J Biol Inorg Chem. 2004 Apr; 9(3):297-306. PMID: 14770302.
      Citations: 3     Fields:    Translation:Cells
    46. 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. 2003 Nov 25; 42(46):13625-36. PMID: 14622009.
      Citations: 13     Fields:    Translation:Cells
    47. Emerson JP, Coulter ED, Phillips RS, Kurtz DM. Kinetics of the superoxide reductase catalytic cycle. J Biol Chem. 2003 Oct 10; 278(41):39662-8. PMID: 12900405.
      Citations: 14     Fields:    Translation:AnimalsCells
    48. 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. 2003 May 27; 42(20):6201-8. PMID: 12755623.
      Citations: 3     Fields:    Translation:Cells
    49. 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. J Biol Inorg Chem. 2003 Jul; 8(6):671-82. PMID: 12764688.
      Citations: 7     Fields:    Translation:Cells
    50. 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. 2003 Mar 18; 42(10):2806-15. PMID: 12627946.
      Citations: 35     Fields:    Translation:Cells
    51. 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. Proc Natl Acad Sci U S A. 2003 Apr 01; 100(7):3802-7. PMID: 12637682.
      Citations: 15     Fields:    Translation:Cells
    52. 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. Inorg Chem. 2003 Jan 27; 42(2):446-56. PMID: 12693226.
      Citations: 14     Fields:    Translation:Cells
    53. Cosper NJ, Eby DM, Kounosu A, Kurosawa N, Neidle EL, Kurtz DM, Iwasaki T, Scott RA. Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters. Protein Sci. 2002 Dec; 11(12):2969-73. PMID: 12441394.
      Citations: 8     Fields:    Translation:Cells
    54. 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. J Am Chem Soc. 2002 Aug 21; 124(33):9845-55. PMID: 12175244.
      Citations: 21     Fields:    Translation:Cells
    55. Karlsson A, Beharry ZM, Matthew Eby D, Coulter ED, Neidle EL, Kurtz DM, Eklund H, Ramaswamy S. X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1. J Mol Biol. 2002 Apr 26; 318(2):261-72. PMID: 12051836.
      Citations: 16     Fields:    Translation:Cells
    56. Kurtz DM, Coulter ED. The mechanism(s) of superoxide reduction by superoxide reductases in vitro and in vivo. J Biol Inorg Chem. 2002 Jun; 7(6):653-8. PMID: 12072973.
      Citations: 10     Fields:    Translation:Cells
    57. 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. 2002 Apr 02; 41(13):4348-57. PMID: 11914081.
      Citations: 28     Fields:    Translation:Cells
    58. Sztukowska M, Bugno M, Potempa J, Travis J, Kurtz DM. Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis. Mol Microbiol. 2002 Apr; 44(2):479-88. PMID: 11972784.
      Citations: 44     Fields:    Translation:Cells
    59. 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. J Biol Inorg Chem. 2002 Apr; 7(4-5):427-36. PMID: 11941500.
      Citations: 5     Fields:    Translation:Cells
    60. 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. Arch Biochem Biophys. 2001 Oct 01; 394(1):76-86. PMID: 11566030.
      Citations: 34     Fields:    Translation:Cells
    61. Farmer CS, Kurtz DM, Liu ZJ, Wang BC, Rose J, Ai J, Sanders-Loehr J. The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket. J Biol Inorg Chem. 2001 Apr; 6(4):418-29. PMID: 11372200.
      Citations: 10     Fields:    Translation:AnimalsCells
    62. Das A, Coulter ED, Kurtz DM, Ljungdahl LG. Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase- rubredoxin and rubrerythrin-type A flavoprotein- high-molecular-weight rubredoxin. J Bacteriol. 2001 Mar; 183(5):1560-7. PMID: 11160086.
      Citations: 19     Fields:    Translation:Cells
    63. Taylor PK, Parks BA, Kurtz DM, Amster IJ. Analysis of metal incorporation during overexpression of Clostridium pasteurianum rubredoxin by electrospray FTICR mass spectrometry. J Biol Inorg Chem. 2001 Feb; 6(2):201-6. PMID: 11293415.
      Citations: 4     Fields:    Translation:Cells
    64. Lumppio HL, Shenvi NV, Summers AO, Voordouw G, Kurtz DM. Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system. J Bacteriol. 2001 Jan; 183(1):101-8. PMID: 11114906.
      Citations: 67     Fields:    Translation:Cells
    65. Eby DM, Beharry ZM, Coulter ED, Kurtz DM, Neidle EL. Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1. J Bacteriol. 2001 Jan; 183(1):109-18. PMID: 11114907.
      Citations: 18     Fields:    Translation:Cells
    66. Bonomi F, Fessas D, Iametti S, Kurtz DM, Mazzini S. Thermal stability of Clostridium pasteurianum rubredoxin: deconvoluting the contributions of the metal site and the protein. Protein Sci. 2000 Dec; 9(12):2413-26. PMID: 11206063.
      Citations: 5     Fields:    Translation:Cells
    67. Kurtz DM, Tian L, Gower BA, Nagy TR, Pinkert CA, Wood PA. Transgenic studies of fatty acid oxidation gene expression in nonobese diabetic mice. J Lipid Res. 2000 Dec; 41(12):2063-70. PMID: 11108740.
      Citations: 2     Fields:    Translation:AnimalsCells
    68. Xiong J, Phillips RS, Kurtz DM, Jin S, Ai J, Sanders-Loehr J. The O(2) binding pocket of myohemerythrin: role of a conserved leucine. Biochemistry. 2000 Jul 25; 39(29):8526-36. PMID: 10913259.
      Citations: 10     Fields:    Translation:AnimalsCells
    69. Farmer CS, Kurtz DM, Phillips RS, Ai J, Sanders-Loehr J. A leucine residue "Gates" solvent but not O2 access to the binding pocket of phascolopsis gouldii hemerythrin. J Biol Chem. 2000 Jun 02; 275(22):17043-50. PMID: 10748012.
      Citations: 8     Fields:    Translation:AnimalsCells
    70. Xiong J, Kurtz DM, Ai J, Sanders-Loehr J. A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry. 2000 May 02; 39(17):5117-25. PMID: 10819979.
      Citations: 27     Fields:    Translation:Cells
    71. Eidsness MK, Burden AE, Richie KA, Kurtz DM, Scott RA, Smith ET, Ichiye T, Beard B, Min T, Kang C. Modulation of the redox potential of the [Fe(SCys)(4)] site in rubredoxin by the orientation of a peptide dipole. Biochemistry. 1999 Nov 09; 38(45):14803-9. PMID: 10555962.
      Citations: 27     Fields:    Translation:Cells
    72. Coulter ED, Shenvi NV, Kurtz DM. NADH peroxidase activity of rubrerythrin. Biochem Biophys Res Commun. 1999 Feb 16; 255(2):317-23. PMID: 10049706.
      Citations: 20     Fields:    Translation:Cells
    73. Kurtz DM. Oxygen-carrying proteins: three solutions to a common problem. Essays Biochem. 1999; 34:85-100. PMID: 10730190.
      Citations: 13     Fields:    Translation:HumansAnimalsCells
    74. Kurtz DM, Rinaldo P, Rhead WJ, Tian L, Millington DS, Vockley J, Hamm DA, Brix AE, Lindsey JR, Pinkert CA, O'Brien WE, Wood PA. Targeted disruption of mouse long-chain acyl-CoA dehydrogenase gene reveals crucial roles for fatty acid oxidation. Proc Natl Acad Sci U S A. 1998 Dec 22; 95(26):15592-7. PMID: 9861014.
      Citations: 57     Fields:    Translation:HumansAnimalsCells
    75. Guerra C, Koza RA, Walsh K, Kurtz DM, Wood PA, Kozak LP. Abnormal nonshivering thermogenesis in mice with inherited defects of fatty acid oxidation. J Clin Invest. 1998 Nov 01; 102(9):1724-31. PMID: 9802886.
      Citations: 46     Fields:    Translation:AnimalsCells
    76. Lei QP, Cui X, Kurtz DM, Amster IJ, Chernushevich IV, Standing KG. Electrospray mass spectrometry studies of non-heme iron-containing proteins. Anal Chem. 1998 May 01; 70(9):1838-46. PMID: 9599583.
      Citations: 10     Fields:    
    77. Eidsness MK, Richie KA, Burden AE, Kurtz DM, Scott RA. Dissecting contributions to the thermostability of Pyrococcus furiosus rubredoxin: beta-sheet chimeras. Biochemistry. 1997 Aug 26; 36(34):10406-13. PMID: 9265620.
      Citations: 22     Fields:    Translation:Cells
    78. Stemmler TL, Sossong TM, Goldstein JI, Ash DE, Elgren TE, Kurtz DM, Penner-Hahn JE. EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganese-substituted ribonucleotide reductase and hemerythrin. Biochemistry. 1997 Aug 12; 36(32):9847-58. PMID: 9245417.
      Citations: 22     Fields:    Translation:Animals
    79. Lumppio HL, Shenvi NV, Garg RP, Summers AO, Kurtz DM. A rubrerythrin operon and nigerythrin gene in Desulfovibrio vulgaris (Hildenborough). J Bacteriol. 1997 Jul; 179(14):4607-15. PMID: 9226272.
      Citations: 11     Fields:    Translation:Cells
    80. deMaré F, Kurtz DM, Nordlund P. The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nat Struct Biol. 1996 Jun; 3(6):539-46. PMID: 8646540.
      Citations: 28     Fields:    Translation:Cells
    81. 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. 1996 May 21; 35(20):6297-301. PMID: 8639572.
      Citations: 23     Fields:    Translation:Cells
    82. Tolwani RJ, Farmer SC, Johnson KR, Davisson MT, Kurtz DM, Hinsdale ME, Cresci S, Kelly DP, Wood PA. Structure and chromosomal location of the mouse medium-chain acyl-CoA dehydrogenase-encoding gene and its promoter. Gene. 1996 May 08; 170(2):165-71. PMID: 8666240.
      Citations: 6     Fields:    Translation:HumansAnimalsCells
    83. Richie KA, Teng Q, Elkin CJ, Kurtz DM. 2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to thermostability. Protein Sci. 1996 May; 5(5):883-94. PMID: 8732760.
      Citations: 11     Fields:    Translation:Cells
    84. Gupta N, Bonomi F, Kurtz DM, Ravi N, Wang DL, Huynh BH. Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain. Biochemistry. 1995 Mar 14; 34(10):3310-8. PMID: 7880826.
      Citations: 14     Fields:    Translation:Cells
    85. Negri A, Tedeschi G, Bonomi F, Zhang JH, Kurtz DM. Amino-acid sequences of the alpha- and beta-subunits of hemerythrin from Lingula reevii. Biochim Biophys Acta. 1994 Oct 19; 1208(2):277-85. PMID: 7947959.
      Citations: 3     Fields:    Translation:AnimalsCells
    86. Dave BC, Czernuszewicz RS, Prickril BC, Kurtz DM. Resonance Raman spectroscopic evidence for the FeS4 and Fe-O-Fe sites in rubrerythrin from Desulfovibrio vulgaris. Biochemistry. 1994 Mar 29; 33(12):3572-6. PMID: 8142354.
      Citations: 7     Fields:    Translation:Cells
    87. Bormett RW, Smith GD, Asher SA, Barrick D, Kurtz DM. Vibrational circular dichroism measurements of ligand vibrations in haem and non-haem metalloenzymes. Faraday Discuss. 1994; (99):327-39; discussion 383-400. PMID: 7549543.
      Citations: 1     Fields:    
    88. 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. 1993 Aug 24; 32(33):8487-91. PMID: 8395205.
      Citations: 5     Fields:    Translation:Cells
    89. Zhang JH, Kurtz DM, Xia YM, Debrunner PG. Conversion of non-functional to functional iron following reconstitution of hemerythrin. Biochim Biophys Acta. 1992 Aug 21; 1122(3):293-8. PMID: 1504090.
      Citations:    Fields:    Translation:Cells
    90. Zhang JH, Kurtz DM. Metal substitutions at the diiron sites of hemerythrin and myohemerythrin: contributions of divalent metals to stability of a four-helix bundle protein. Proc Natl Acad Sci U S A. 1992 Aug 01; 89(15):7065-9. PMID: 1496001.
      Citations: 6     Fields:    Translation:Cells
    91. Long RC, Zhang JH, Kurtz DM, Negri A, Tedeschi G, Bonomi F. Myohemerythrin from the sipunculid, Phascolopsis gouldii: purification, properties and amino acid sequence. Biochim Biophys Acta. 1992 Jul 31; 1122(2):136-42. PMID: 1322702.
      Citations: 2     Fields:    Translation:AnimalsCells
    92. Eidsness MK, O'Dell SE, Kurtz DM, Robson RL, Scott RA. Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasteurianum rubredoxin. Protein Eng. 1992 Jun; 5(4):367-71. PMID: 1409558.
      Citations: 12     Fields:    Translation:Cells
    93. Kurtz DM, Prickril BC. Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris: identification of potential ligands to the diiron site. Biochem Biophys Res Commun. 1991 Nov 27; 181(1):337-41. PMID: 1958203.
      Citations: 9     Fields:    Translation:Cells
    94. Prickril BC, Kurtz DM, LeGall J, Voordouw G. Cloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenborough). Biochemistry. 1991 Nov 19; 30(46):11118-23. PMID: 1932032.
      Citations: 5     Fields:    Translation:Cells
    95. Zhang JH, Kurtz DM. Two distinct subunits of hemerythrin from the brachiopod Lingula reevii: an apparent requirement for cooperativity in O2 binding. Biochemistry. 1991 Sep 24; 30(38):9121-5. PMID: 1892823.
      Citations: 1     Fields:    Translation:AnimalsCells
    96. Zhang JH, Kurtz DM, Xia YM, Debrunner PG. Reconstitution of the diiron sites in hemerythrin and myohemerythrin. Biochemistry. 1991 Jan 15; 30(2):583-9. PMID: 1988045.
      Citations: 6     Fields:    Translation:Animals
    97. Bonomi F, Long RC, Kurtz DM. Purification and properties of a membrane-bound NADH-cytochrome-b5 reductase from erythrocytes of the sipunculid worm, Phascolopsis gouldii. Biochim Biophys Acta. 1989 Nov 30; 999(2):147-56. PMID: 2597703.
      Citations: 4     Fields:    Translation:AnimalsCells
    98. Miller LL, Jacobson RA, Chen YS, Kurtz DM. Structure of hexakis(N-methylimidazole-N')iron(II) tetraphenylborate dichloromethane solvate. Acta Crystallogr C. 1989 Mar 15; 45 ( Pt 3):527-9. PMID: 2610977.
      Citations:    Fields:    Translation:Cells
    99. Krieger J, Schmidt M, Sforza E, Lehr L, Imbs JL, Coumaros G, Kurtz D. Urinary excretion of guanosine 3':5'-cyclic monophosphate during sleep in obstructive sleep apnoea patients with and without nasal continuous positive airway pressure treatment. Clin Sci (Lond). 1989 Jan; 76(1):31-7. PMID: 2537703.
      Citations: 2     Fields:    Translation:Humans
    100. Robitaille PM, Kurtz DM. 31P NMR probes of sipunculan erythrocytes containing the O2-carrying protein hemerythrin. Biochemistry. 1988 Jun 14; 27(12):4458-65. PMID: 3166989.
      Citations: 1     Fields:    Translation:AnimalsCells
    101. Utecht RE, Kurtz DM. Cytochrome b5 and NADH-cytochrome-b5 reductase from sipunculan erythrocytes; a methemerythrin reduction system from Phascolopsis gouldii. Biochim Biophys Acta. 1988 Mar 23; 953(2):164-78. PMID: 2831990.
      Citations: 1     Fields:    Translation:AnimalsCells
    102. 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. 1988 Feb 09; 27(3):1014-24. PMID: 3365363.
      Citations: 12     Fields:    Translation:AnimalsCells
    103. Pearce LL, Utecht RE, Kurtz DM. Comparisons of redox kinetics of methemerythrin and mu-sulfidomethemerythrin. Implications for interactions with cytochrome b5. Biochemistry. 1987 Dec 29; 26(26):8709-17. PMID: 2831950.
      Citations:    Fields:    Translation:AnimalsCells
    104. Bonomi F, Pagani S, Kurtz DM. Enzymic synthesis of the 4Fe-4S clusters of Clostridium pasteurianum ferredoxin. Eur J Biochem. 1985 Apr 01; 148(1):67-73. PMID: 2983992.
      Citations: 12     Fields:    Translation:Cells
    105. 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. 1984 Dec 18; 23(26):6416-22. PMID: 6529557.
      Citations:    Fields:    Translation:AnimalsCells
    106. Nocek JM, Kurtz DM, Pickering RA, Doyle MP. Oxidation of deoxyhemerythrin to semi-methemerythrin by nitrite. J Biol Chem. 1984 Oct 25; 259(20):12334-8. PMID: 6092330.
      Citations: 5     Fields:    Translation:AnimalsCells
    107. 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. Anal Biochem. 1984 Oct; 142(1):226-31. PMID: 6517316.
      Citations: 1     Fields:    Translation:Cells
    108. Kurtz DM, Sage JT, Hendrich M, Debrunner PG, Lukat GS. Semi-met oxidation level of chalcogenide derivatives of methemerythrin. Mössbauer and EPR studies. J Biol Chem. 1983 Feb 25; 258(4):2115-7. PMID: 6296130.
      Citations:    Fields:    Translation:AnimalsCells
    109. 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. 1982 Dec 21; 21(26):6838-43. PMID: 7159566.
      Citations:    Fields:    Translation:AnimalsCells
    110. Kurtz DM. A new method for extrusion of iron-sulfur cores from active centers of proteins. Biochem Biophys Res Commun. 1982 Jan 29; 104(2):437-42. PMID: 7073692.
      Citations:    Fields:    Translation:Animals
    111. Wigler M, Perucho M, Kurtz D, Dana S, Pellicer A, Axel R, Silverstein S. Transformation of mammalian cells with an amplifiable dominant-acting gene. Proc Natl Acad Sci U S A. 1980 Jun; 77(6):3567-70. PMID: 6251468.
      Citations: 49     Fields:    Translation:AnimalsCells
    112. Kurtz DM, McMillan RS, Burgess BK, Mortenson LE, Holm RH. Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase. Proc Natl Acad Sci U S A. 1979 Oct; 76(10):4986-9. PMID: 291915.
      Citations: 10     Fields:    Translation:Cells
    113. Coles CJ, Holm RH, Kurtz DM, Orme-Johnson WH, Rawlings J, Singer TP, Wong GB. Characterization of the iron-sulfur centers in succinate dehydrogenase. Proc Natl Acad Sci U S A. 1979 Aug; 76(8):3805-8. PMID: 226982.
      Citations: 4     Fields:    Translation:Cells
    114. 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. J Biol Chem. 1979 Jun 25; 254(12):4967-9. PMID: 447628.
      Citations: 8     Fields:    Translation:AnimalsCells
    115. Kurtz DM, Shriver DF, Klotz IM. Letter: Resonance raman spectroscopy with unsymmetrically isotopic ligands. Differentiation of possible structures of hemerythrin complexes. J Am Chem Soc. 1976 Aug 04; 98(16):5033-5. PMID: 950426.
      Citations: 5     Fields:    
    Kurtz's Networks
    Click the
    Explore
    buttons for more information and interactive visualizations!
    Concepts (365)
    Explore
    _
    Co-Authors (1)
    Explore
    _
    Similar People (60)
    Explore
    _
    Same Department Expand Description
    Explore
    _
    RCMI CC is supported by the National Institute on Minority Health and Health Disparities, National Institutes of Health (NIH), through Grant Number U24MD015970. The contents of this site are solely the responsibility of the authors and do not necessarily represent the official views of the NIH

    For technical support please contact support