title: The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.
abstract: Nature is a valuable source of inspiration in the design of catalysts, and various approaches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H2. In FeFe hydrogenases, H2 oxidation occurs at the H-cluster, and catalysis involves H2 binding on the vacant coordination site of an iron centre. Here, we show that the reversible oxidative inactivation of this enzyme results from the binding of H2 to coordination positions that are normally blocked by intrinsic CO ligands. This flexibility of the coordination sphere around the reactive iron centre confers on the enzyme the ability to avoid harmful reactions under oxidizing conditions, including exposure to O2. The versatile chemistry of the diiron cluster in the natural system might inspire the design of novel synthetic catalysts for H2 oxidation.
authors.affiliation: Aix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
authors.forename: Vincent
authors.initials: V
authors.lastname: Fourmond
authors.affiliation: Department of Earth and Environmental Science, Università degli Studi di Milano-Bicocca, P.zza della Scienza 1, Milan 20126, Italy.
authors.forename: Claudio
authors.initials: C
authors.lastname: Greco
authors.affiliation: iBiTec-S, SB2SM, LMB (UMR CNRS 8221), DSV, CEA, 91191 Gif-sur-Yvette, France.
authors.forename: Kateryna
authors.initials: K
authors.lastname: Sybirna
authors.affiliation: Aix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
authors.forename: Carole
authors.initials: C
authors.lastname: Baffert
authors.affiliation: University College London, Department of Physics and Astronomy, Gower Street, London WC1E 6BT, UK.
authors.forename: Po-Hung
authors.initials: PH
authors.lastname: Wang
authors.affiliation: Aix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Ezanno
authors.affiliation: University College London, Department of Physics and Astronomy, Gower Street, London WC1E 6BT, UK.
authors.forename: Marco
authors.initials: M
authors.lastname: Montefiori
authors.affiliation: Department of Earth and Environmental Science, Università degli Studi di Milano-Bicocca, P.zza della Scienza 1, Milan 20126, Italy.
authors.forename: Maurizio
authors.initials: M
authors.lastname: Bruschi
authors.affiliation: Université de Toulouse, INSA, UPS, INP, LISBP, INRA:UMR792,135 CNRS:UMR 5504, avenue de Rangueil, 31077 Toulouse, France.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Meynial-Salles
authors.affiliation: Université de Toulouse, INSA, UPS, INP, LISBP, INRA:UMR792,135 CNRS:UMR 5504, avenue de Rangueil, 31077 Toulouse, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: Soucaille
authors.affiliation: University College London, Department of Physics and Astronomy, Gower Street, London WC1E 6BT, UK.
authors.forename: Jochen
authors.initials: J
authors.lastname: Blumberger
authors.affiliation: iBiTec-S, SB2SM, LMB (UMR CNRS 8221), DSV, CEA, 91191 Gif-sur-Yvette, France.
authors.forename: Hervé
authors.initials: H
authors.lastname: Bottin
authors.affiliation: Department of Biotechnology and Biosciences, Università degli Studi di Milano-Bicocca, P.zza della Scienza 2, Milan 20126, Italy.
authors.forename: Luca
authors.initials: L
authors.lastname: De Gioia
authors.affiliation: Aix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Léger
mesh_terms: D006859:Hydrogen / Q000737:chemistry; D006864:Hydrogenase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry; D007700:Kinetics; D009154:Mutation; D010084:Oxidation-Reduction; D010649:Phenylalanine / Q000737:chemistry; D011487:Protein Conformation; D014443:Tyrosine / Q000737:chemistry
chemical_list: D007506:Iron-Sulfur Proteins; D014443:Tyrosine; D010649:Phenylalanine; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase