title: A novel FeS cluster in Fe-only hydrogenases.
abstract: Many microorganisms can use molecular hydrogen as a source of electrons or generate it by reducing protons. These reactions are catalysed by metalloenzymes of two types: NiFe and Fe-only hydrogenases. Here, we review recent structural results concerning the latter, putting special emphasis on the characteristics of the active site.
authors.affiliation: Laboratoire de Cristallographie et de Cristallogenèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS, 41 Avenue des Martyrs, 38027, Grenoble Cedex 1, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Nicolet
authors.forename: B J
authors.initials: BJ
authors.lastname: Lemon
authors.forename: J C
authors.initials: JC
authors.lastname: Fontecilla-Camps
authors.forename: J W
authors.initials: JW
authors.lastname: Peters
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry; D003593:Cytoplasm / Q000201:enzymology; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019897:Periplasm / Q000201:enzymology; D011487:Protein Conformation; D013455:Sulfur / Q000737:chemistry*; D014867:Water
chemical_list: D014867:Water; D013455:Sulfur; D007501:Iron; D006864:Hydrogenase; D003545:Cysteine