title: Structure-function relationships in [FeFe]-hydrogenase active site maturation.
abstract: Since the discovery that, despite the active site complexity, only three gene products suffice to obtain active recombinant [FeFe]-hydrogenase, significant light has been shed on this process. Both the source of the CO and CN(-) ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. From both spectroscopy and model chemistry, it is predicted that an amine function in this ligand plays a central role in catalysis, acting as a base in the heterolytic cleavage of hydrogen.
authors.affiliation: Metalloproteins Unit, Institut de Biologie Structurale Jean-Pierre Ebel, Commissariat à l'Energie Atomique, CNRS, Université Joseph Fourier, 38027 Grenoble Cedex 1, France.
authors.forename: Yvain
authors.initials: Y
authors.lastname: Nicolet
authors.forename: Juan C
authors.initials: JC
authors.lastname: Fontecilla-Camps
mesh_terms: D000465:Algorithms; D001671:Biochemistry / Q000379:methods; D002384:Catalysis; D020134:Catalytic Domain; D002696:Chlamydomonas / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D005872:Giardia / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry; D006864:Hydrogenase / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013053:Spectrophotometry / Q000379:methods; D013329:Structure-Activity Relationship; D020124:Thermotoga maritima / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D007506:Iron-Sulfur Proteins; D008024:Ligands; D011994:Recombinant Proteins; D015534:Trans-Activators; C423908:zraR protein, E coli; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase