title: Structure and mechanism of iron-only hydrogenases.
abstract: The recent elucidation of the structures of iron-only hydrogenases from the microorganisms Clostridium pasteurianum and Desulfovibrio desulfuricans has revealed that the presumed site of reversible hydrogen oxidation exists as a unique, protein-associated organometallic prosthetic group. Details of the hydrogenase structures provide insight into the chemical mechanism of this highly evolved catalyst.
authors.affiliation: Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322-0300, USA. petersj@cc.usu.edu
authors.forename: J W
authors.initials: JW
authors.lastname: Peters
mesh_terms: D001665:Binding Sites; D004579:Electron Transport; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D007506:Iron-Sulfur Proteins; C118830:iron hydrogenase; D006864:Hydrogenase