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Journal Abstract Search

143 related items for PubMed ID: 8026480

  • 1. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein.
    Trautwein T, Krauss F, Lottspeich F, Simon H.
    Eur J Biochem; 1994 Jun 15; 222(3):1025-32. PubMed ID: 8026480
    [Abstract] [Full Text] [Related]

  • 2. Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor.
    Hanlon SP, Toh TH, Solomon PS, Holt RA, McEwan AG.
    Eur J Biochem; 1996 Jul 15; 239(2):391-6. PubMed ID: 8706745
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  • 3. Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.
    McEwan AG, Ferguson SJ, Jackson JB.
    Biochem J; 1991 Feb 15; 274 ( Pt 1)(Pt 1):305-7. PubMed ID: 2001248
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  • 4. The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.
    Yokoyama K, Leimkühler S.
    Biochim Biophys Acta; 2015 Jun 15; 1853(6):1335-49. PubMed ID: 25268953
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  • 6. Microbial metabolism of quinoline and related compounds. XVI. Quinaldine oxidoreductase from Arthrobacter spec. Rü 61a: a molybdenum-containing enzyme catalysing the hydroxylation at C-4 of the heterocycle.
    de Beyer A, Lingens F.
    Biol Chem Hoppe Seyler; 1993 Feb 15; 374(2):101-9. PubMed ID: 8471177
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  • 8. Characterisation of the pterin molybdenum cofactor in dimethylsulfoxide reductase of Rhodobacter capsulatus.
    Solomon PS, Lane I, Hanson GR, McEwan AG.
    Eur J Biochem; 1997 May 15; 246(1):200-3. PubMed ID: 9210484
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  • 10. Molybdenum-cofactor-containing enzymes: structure and mechanism.
    Kisker C, Schindelin H, Rees DC.
    Annu Rev Biochem; 1997 May 15; 66():233-67. PubMed ID: 9242907
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  • 11. The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor.
    Karrasch M, Börner G, Enssle M, Thauer RK.
    Eur J Biochem; 1990 Dec 12; 194(2):367-72. PubMed ID: 2125267
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  • 12. Microbial metabolism of quinoline and related compounds. XV. Quinoline-4-carboxylic acid oxidoreductase from Agrobacterium spec.1B: a molybdenum-containing enzyme.
    Bauer G, Lingens F.
    Biol Chem Hoppe Seyler; 1992 Aug 12; 373(8):699-705. PubMed ID: 1418685
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  • 13. Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
    Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC.
    Science; 1996 Jun 14; 272(5268):1615-21. PubMed ID: 8658134
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  • 14. Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1.
    Fetzner S, Lingens F.
    Biol Chem Hoppe Seyler; 1993 Jun 14; 374(6):363-76. PubMed ID: 8357532
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  • 15. Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity.
    Weiner JH, MacIsaac DP, Bishop RE, Bilous PT.
    J Bacteriol; 1988 Apr 14; 170(4):1505-10. PubMed ID: 3280546
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  • 17. Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases.
    Sauter M, Tshisuaka B, Fetzner S, Lingens F.
    Biol Chem Hoppe Seyler; 1993 Nov 14; 374(11):1037-46. PubMed ID: 8292263
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  • 18. The tungsten-containing aldehyde oxidoreductase from Clostridium thermoaceticum and its complex with a viologen-accepting NADPH oxidoreductase.
    Strobl G, Feicht R, White H, Lottspeich F, Simon H.
    Biol Chem Hoppe Seyler; 1992 Mar 14; 373(3):123-32. PubMed ID: 1586452
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  • 20. Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the xanthine oxidase family: mechanistic implications.
    Canne C, Lowe DJ, Fetzner S, Adams B, Smith AT, Kappl R, Bray RC, Hüttermann J.
    Biochemistry; 1999 Oct 19; 38(42):14077-87. PubMed ID: 10529255
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