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Nat Chem Biol. 2013 Jan;9(1):15-7. doi: 10.1038/nchembio.1110. Epub 2012 Nov 11.

O2-independent formation of the inactive states of NiFe hydrogenase.

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  • 1Aix-Marseille Université, Centre National de la Recherche Scientifique (CNRS), Laboratoire de Bioénergétique et Ingénierie des Protéines, Unité Mixte de Recherche 7281, Institut de Microbiologie de la Méditerranée, Marseille, France.

Abstract

We studied the mechanism of aerobic inactivation of Desulfovibrio fructosovorans nickel-iron (NiFe) hydrogenase by quantitatively examining the results of electrochemistry, EPR and FTIR experiments. They suggest that, contrary to the commonly accepted mechanism, the attacking O(2) is not incorporated as an active site ligand but, rather, acts as an electron acceptor. Our findings offer new ways toward the understanding of O(2) inactivation and O(2) tolerance in NiFe hydrogenases.

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PMID:
23143415
DOI:
10.1038/nchembio.1110
[PubMed - indexed for MEDLINE]
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