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225 related items for PubMed ID: 8174563

  • 1. On the iron-sulfur cluster of adenosine phosphosulfate reductase from Desulfovibrio vulgaris (Hildenborough).
    Verhagen MF, Kooter IM, Wolbert RB, Hagen WR.
    Eur J Biochem; 1994 Apr 15; 221(2):831-7. PubMed ID: 8174563
    [Abstract] [Full Text] [Related]

  • 2. The active centers of adenylylsulfate reductase from Desulfovibrio gigas. Characterization and spectroscopic studies.
    Lampreia J, Moura I, Teixeira M, Peck HD, Legall J, Huynh BH, Moura JJ.
    Eur J Biochem; 1990 Mar 30; 188(3):653-64. PubMed ID: 2158885
    [Abstract] [Full Text] [Related]

  • 3. Adenylylsulfate reductases from archaea and bacteria are 1:1 alphabeta-heterodimeric iron-sulfur flavoenzymes--high similarity of molecular properties emphasizes their central role in sulfur metabolism.
    Fritz G, Büchert T, Huber H, Stetter KO, Kroneck PM.
    FEBS Lett; 2000 May 04; 473(1):63-6. PubMed ID: 10802060
    [Abstract] [Full Text] [Related]

  • 4. Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase.
    Chen L, Le Gall J, Xavier AV.
    Biochem Biophys Res Commun; 1994 Sep 15; 203(2):839-44. PubMed ID: 8093065
    [Abstract] [Full Text] [Related]

  • 5. S = 9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase.
    Pierik AJ, Hagen WR.
    Eur J Biochem; 1991 Jan 30; 195(2):505-16. PubMed ID: 1847685
    [Abstract] [Full Text] [Related]

  • 6. The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters.
    Arendsen AF, Verhagen MF, Wolbert RB, Pierik AJ, Stams AJ, Jetten MS, Hagen WR.
    Biochemistry; 1993 Oct 05; 32(39):10323-30. PubMed ID: 8399175
    [Abstract] [Full Text] [Related]

  • 7. Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough).
    Pierik AJ, Hagen WR, Redeker JS, Wolbert RB, Boersma M, Verhagen MF, Grande HJ, Veeger C, Mutsaers PH, Sands RH.
    Eur J Biochem; 1992 Oct 01; 209(1):63-72. PubMed ID: 1396719
    [Abstract] [Full Text] [Related]

  • 8. Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex) and comparison with the enzyme from Desulfovibrio vulgaris (Hildenborough).
    Steuber J, Arendsen AF, Hagen WR, Kroneck PM.
    Eur J Biochem; 1995 Nov 01; 233(3):873-9. PubMed ID: 8521853
    [Abstract] [Full Text] [Related]

  • 9. The function of the [4Fe-4S] clusters and FAD in bacterial and archaeal adenylylsulfate reductases. Evidence for flavin-catalyzed reduction of adenosine 5'-phosphosulfate.
    Fritz G, Büchert T, Kroneck PM.
    J Biol Chem; 2002 Jul 19; 277(29):26066-73. PubMed ID: 12006599
    [Abstract] [Full Text] [Related]

  • 10. Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties.
    Beckmann JD, Frerman FE.
    Biochemistry; 1985 Jul 16; 24(15):3913-21. PubMed ID: 4052375
    [Abstract] [Full Text] [Related]

  • 11. Desulfoviridin, a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies.
    Wolfe BM, Lui SM, Cowan JA.
    Eur J Biochem; 1994 Jul 01; 223(1):79-89. PubMed ID: 8033912
    [Abstract] [Full Text] [Related]

  • 12. The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters.
    Staples CR, Ameyibor E, Fu W, Gardet-Salvi L, Stritt-Etter AL, Schürmann P, Knaff DB, Johnson MK.
    Biochemistry; 1996 Sep 03; 35(35):11425-34. PubMed ID: 8784198
    [Abstract] [Full Text] [Related]

  • 13. Characterization of a sulfite reductase from Desulfovibrio vulgaris. Evidence for the presence of a low-spin siroheme and an exchange-coupled siroheme-[4Fe-4S] unit.
    Huynh BH, Kang L, DerVartanian DV, Peck HD, LeGall J.
    J Biol Chem; 1984 Dec 25; 259(24):15373-6. PubMed ID: 6096368
    [Abstract] [Full Text] [Related]

  • 14. Plant adenosine 5'-phosphosulfate reductase is a novel iron-sulfur protein.
    Kopriva S, Büchert T, Fritz G, Suter M, Weber M, Benda R, Schaller J, Feller U, Schürmann P, Schünemann V, Trautwein AX, Kroneck PM, Brunold C.
    J Biol Chem; 2001 Nov 16; 276(46):42881-6. PubMed ID: 11553635
    [Abstract] [Full Text] [Related]

  • 15. Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups.
    Christner JA, Münck E, Janick PA, Siegel LM.
    J Biol Chem; 1981 Mar 10; 256(5):2098-101. PubMed ID: 6257697
    [Abstract] [Full Text] [Related]

  • 16. Electron paramagnetic resonance and magnetic circular dichroism studies of electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver.
    Johnson MK, Morningstar JE, Oliver M, Frerman FE.
    FEBS Lett; 1987 Dec 21; 226(1):129-33. PubMed ID: 2826249
    [Abstract] [Full Text] [Related]

  • 17. Dissimilatory sulfite reductase revisited. The desulfoviridin molecule does contain 20 iron ions, extensively demetallated sirohaem, and an S = 9/2 iron-sulfur cluster.
    Marritt SJ, Hagen WF.
    Eur J Biochem; 1996 Jun 15; 238(3):724-7. PubMed ID: 8706673
    [Abstract] [Full Text] [Related]

  • 18. Impact of mutations on the midpoint potential of the [4Fe-4S]+1,+2 cluster and on catalytic activity in electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO).
    Usselman RJ, Fielding AJ, Frerman FE, Watmough NJ, Eaton GR, Eaton SS.
    Biochemistry; 2008 Jan 08; 47(1):92-100. PubMed ID: 18069858
    [Abstract] [Full Text] [Related]

  • 19. The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein.
    Swanson MA, Usselman RJ, Frerman FE, Eaton GR, Eaton SS.
    Biochemistry; 2008 Aug 26; 47(34):8894-901. PubMed ID: 18672901
    [Abstract] [Full Text] [Related]

  • 20. Multi-frequency EPR and high-resolution Mössbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Characterization of a supercluster and superspin model protein.
    Pierik AJ, Hagen WR, Dunham WR, Sands RH.
    Eur J Biochem; 1992 Jun 15; 206(3):705-19. PubMed ID: 1318833
    [Abstract] [Full Text] [Related]

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