Document Detail

O(2)-independent formation of the inactive states of NiFe hydrogenase.
MedLine Citation:
PMID:  23143415     Owner:  NLM     Status:  Publisher    
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.
Abbas Abou Hamdan; Bénédicte Burlat; Oscar Gutiérrez-Sanz; Pierre-Pol Liebgott; Carole Baffert; Antonio L De Lacey; Marc Rousset; Bruno Guigliarelli; Christophe Léger; Sébastien Dementin
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-11
Journal Detail:
Title:  Nature chemical biology     Volume:  -     ISSN:  1552-4469     ISO Abbreviation:  Nat. Chem. Biol.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101231976     Medline TA:  Nat Chem Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Aix-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.
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