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152 related items for PubMed ID: 23215250

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  • 6. Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas.
    Cordas CM, Moura I, Moura JJ.
    Bioelectrochemistry; 2008 Nov; 74(1):83-9. PubMed ID: 18632311
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  • 12. Oriented immobilization of a membrane-bound hydrogenase onto an electrode for direct electron transfer.
    Gutiérrez-Sánchez C, Olea D, Marques M, Fernández VM, Pereira IA, Vélez M, De Lacey AL.
    Langmuir; 2011 May 17; 27(10):6449-57. PubMed ID: 21491850
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  • 13. Pathways of H2 toward the active site of [NiFe]-hydrogenase.
    Teixeira VH, Baptista AM, Soares CM.
    Biophys J; 2006 Sep 15; 91(6):2035-45. PubMed ID: 16731562
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  • 14. Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F.
    Foerster S, Stein M, Brecht M, Ogata H, Higuchi Y, Lubitz W.
    J Am Chem Soc; 2003 Jan 08; 125(1):83-93. PubMed ID: 12515509
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  • 15. EPR experiments to elucidate the structure of the ready and unready states of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F.
    van Gastel M, Fichtner C, Neese F, Lubitz W.
    Biochem Soc Trans; 2005 Feb 08; 33(Pt 1):7-11. PubMed ID: 15667250
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  • 16. The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated" state.
    Marques MC, Coelho R, De Lacey AL, Pereira IA, Matias PM.
    J Mol Biol; 2010 Mar 05; 396(4):893-907. PubMed ID: 20026074
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  • 18. Photosensitivity of the Ni-A state of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F with visible light.
    Osuka H, Shomura Y, Komori H, Shibata N, Nagao S, Higuchi Y, Hirota S.
    Biochem Biophys Res Commun; 2013 Jan 04; 430(1):284-8. PubMed ID: 23159801
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  • 20. Liberation of hydrogen sulfide during the catalytic action of Desulfovibrio hydrogenase under the atmosphere of hydrogen.
    Higuchi Y, Yagi T.
    Biochem Biophys Res Commun; 1999 Feb 16; 255(2):295-9. PubMed ID: 10049702
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