title: O2-independent formation of the inactive states of NiFe hydrogenase.
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.
authors.affiliation: 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.
authors.forename: Abbas
authors.initials: A
authors.lastname: Abou Hamdan
authors.forename: Bénédicte
authors.initials: B
authors.lastname: Burlat
authors.forename: Oscar
authors.initials: O
authors.lastname: Gutiérrez-Sanz
authors.forename: Pierre-Pol
authors.initials: PP
authors.lastname: Liebgott
authors.forename: Carole
authors.initials: C
authors.lastname: Baffert
authors.forename: Antonio L
authors.initials: AL
authors.lastname: De Lacey
authors.forename: Marc
authors.initials: M
authors.lastname: Rousset
authors.forename: Bruno
authors.initials: B
authors.lastname: Guigliarelli
authors.forename: Christophe
authors.initials: C
authors.lastname: Léger
authors.forename: Sébastien
authors.initials: S
authors.lastname: Dementin
mesh_terms: D003901:Desulfovibrio / Q000201:enzymology; D055664:Electrochemical Techniques; D004578:Electron Spin Resonance Spectroscopy; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010100:Oxygen