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Connection

Donald Kurtz to Hemerythrin

This is a "connection" page, showing publications Donald Kurtz has written about Hemerythrin.
Connection Strength

3.445
  1. 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.
    View in: PubMed
    Score: 0.577
  2. 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.
    View in: PubMed
    Score: 0.431
  3. 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.
    View in: PubMed
    Score: 0.149
  4. 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.
    View in: PubMed
    Score: 0.124
  5. 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.
    View in: PubMed
    Score: 0.120
  6. 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.
    View in: PubMed
    Score: 0.117
  7. 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.
    View in: PubMed
    Score: 0.116
  8. 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.
    View in: PubMed
    Score: 0.106
  9. Hayashi T, Caranto JD, Matsumura H, Kurtz DM, Mo?nne-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.
    View in: PubMed
    Score: 0.104
  10. 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.
    View in: PubMed
    Score: 0.100
  11. 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.
    View in: PubMed
    Score: 0.092
  12. Riebe O, Fischer RJ, Wampler DA, Kurtz DM, Bahl H. Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum. Microbiology (Reading). 2009 Jan; 155(Pt 1):16-24.
    View in: PubMed
    Score: 0.083
  13. Robitaille PM, Kurtz DM. 31P NMR probes of sipunculan erythrocytes containing the O2-carrying protein hemerythrin. Biochemistry. 1988 Jun 14; 27(12):4458-65.
    View in: PubMed
    Score: 0.080
  14. 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.
    View in: PubMed
    Score: 0.078
  15. 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.
    View in: PubMed
    Score: 0.077
  16. 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.
    View in: PubMed
    Score: 0.070
  17. Kurtz DM. Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin. J Inorg Biochem. 2006 Apr; 100(4):679-93.
    View in: PubMed
    Score: 0.068
  18. 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.
    View in: PubMed
    Score: 0.064
  19. 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.
    View in: PubMed
    Score: 0.056
  20. Kurtz DM, Sage JT, Hendrich M, Debrunner PG, Lukat GS. Semi-met oxidation level of chalcogenide derivatives of methemerythrin. M?ssbauer and EPR studies. J Biol Chem. 1983 Feb 25; 258(4):2115-7.
    View in: PubMed
    Score: 0.055
  21. 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.
    View in: PubMed
    Score: 0.052
  22. 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.
    View in: PubMed
    Score: 0.050
  23. 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.
    View in: PubMed
    Score: 0.048
  24. 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.
    View in: PubMed
    Score: 0.048
  25. 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.
    View in: PubMed
    Score: 0.046
  26. 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.
    View in: PubMed
    Score: 0.046
  27. 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.
    View in: PubMed
    Score: 0.045
  28. Coulter ED, Shenvi NV, Kurtz DM. NADH peroxidase activity of rubrerythrin. Biochem Biophys Res Commun. 1999 Feb 16; 255(2):317-23.
    View in: PubMed
    Score: 0.042
  29. Kurtz DM. Oxygen-carrying proteins: three solutions to a common problem. Essays Biochem. 1999; 34:85-100.
    View in: PubMed
    Score: 0.041
  30. 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.
    View in: PubMed
    Score: 0.038
  31. 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.
    View in: PubMed
    Score: 0.035
  32. 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.
    View in: PubMed
    Score: 0.030
  33. 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.
    View in: PubMed
    Score: 0.027
  34. 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.
    View in: PubMed
    Score: 0.027
  35. 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.
    View in: PubMed
    Score: 0.025
  36. 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.
    View in: PubMed
    Score: 0.024
  37. 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.
    View in: PubMed
    Score: 0.019
  38. 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.
    View in: PubMed
    Score: 0.017
  39. 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.
    View in: PubMed
    Score: 0.016
  40. 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.
    View in: PubMed
    Score: 0.015
  41. 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.
    View in: PubMed
    Score: 0.015
  42. 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.
    View in: PubMed
    Score: 0.015
  43. 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.
    View in: PubMed
    Score: 0.013
  44. 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.
    View in: PubMed
    Score: 0.012
  45. deMar? 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.
    View in: PubMed
    Score: 0.009
  46. 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.
    View in: PubMed
    Score: 0.008
  47. 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.
    View in: PubMed
    Score: 0.007
  48. 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.
    View in: PubMed
    Score: 0.006
Connection Strength

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Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.
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