| Literature DB >> 23143415 |
Abbas Abou Hamdan1, Bénédicte Burlat, Oscar Gutiérrez-Sanz, Pierre-Pol Liebgott, Carole Baffert, Antonio L De Lacey, Marc Rousset, Bruno Guigliarelli, Christophe Léger, Sébastien Dementin.
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.Entities:
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Year: 2012 PMID: 23143415 DOI: 10.1038/nchembio.1110
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040