title: A pyridinol acyl cofactor in the active site of [Fe]-hydrogenase evidenced by the reactivity of model complexes.
abstract: Understanding the complex: The decomposition reaction of a water-soluble complex (see scheme; 1) in H(2)O confirms the existence of a unique bidentate pyridinol cofactor in [Fe]-hydrogenase. This unique moiety is confirmed for the first time by the decomposition of a well-defined model complex containing a pyridinyl methyl acyl ligand.
authors.affiliation: School of Chemical Engineering & Technology, Harbin Institute of Technology, Harbin 150001, PR China.
authors.forename: Bowen
authors.initials: B
authors.lastname: Hu
authors.forename: Dafa
authors.initials: D
authors.lastname: Chen
authors.forename: Xile
authors.initials: X
authors.lastname: Hu
mesh_terms: D002248:Carbon Monoxide / Q000737:chemistry; D002264:Carboxylic Acids / Q000737:chemistry; D020134:Catalytic Domain; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008623:Mercaptoethanol / Q000737:chemistry; D008956:Models, Chemical; D008968:Molecular Conformation; D014466:Ultraviolet Rays
chemical_list: D002264:Carboxylic Acids; D007506:Iron-Sulfur Proteins; D008623:Mercaptoethanol; D002248:Carbon Monoxide; C118830:iron hydrogenase; D006864:Hydrogenase