Hydrogenases and H(+)-reduction in primary energy conservation.
Hydrogenases are metalloenzymes subdivided into two classes that contain iron-sulfur clusters and catalyze the reversible oxidation of hydrogen gas (H(2)[Symbol: see text]left arrow over right arrow[Symbol: see text]2H(+)[Symbol: see text]+[Symbol: see text]2e(-)). Two metal atoms are present at their active center: either a Ni and an Fe atom in the [NiFe]hydrogenases, or two Fe atoms in the [FeFe]hydrogenases. They are phylogenetically distinct classes of proteins. The catalytic core of [NiFe]hydrogenases is a heterodimeric protein associated with additional subunits in many of these enzymes. The catalytic core of [FeFe]hydrogenases is a domain of about 350 residues that accommodates the active site (H cluster). Many [FeFe]hydrogenases are monomeric but possess additional domains that contain redox centers, mostly Fe-S clusters. A third class of hydrogenase, characterized by a specific iron-containing cofactor and by the absence of Fe-S cluster, is found in some methanogenic archaea; this Hmd hydrogenase has catalytic properties different from those of [NiFe]- and [FeFe]hydrogenases. The [NiFe]hydrogenases can be subdivided into four subgroups: (1) the H(2) uptake [NiFe]hydrogenases (group 1); (2) the cyanobacterial uptake hydrogenases and the cytoplasmic H(2) sensors (group 2); (3) the bidirectional cytoplasmic hydrogenases able to bind soluble cofactors (group 3); and (4) the membrane-associated, energy-converting, H(2) evolving hydrogenases (group 4). Unlike the [NiFe]hydrogenases, the [FeFe]hydrogenases form a homogeneous group and are primarily involved in H(2) evolution. This review recapitulates the classification of hydrogenases based on phylogenetic analysis and the correlation with hydrogenase function of the different phylogenetic groupings, discusses the possible role of the [FeFe]hydrogenases in the genesis of the eukaryotic cell, and emphasizes the structural and functional relationships of hydrogenase subunits with those of complex I of the respiratory electron transport chain.
Vignais
Paulette M
PM
Laboratoire de Biochimie et Biophysique des Systèmes Intégrés, UMR CEA/CNRS/UJF no. 5092, Institut de Recherches en Technologies et Sciences pour le Vivant, Grenoble cedex 9, France. p.vignais@wanadoo.fr
D000255:Adenosine Triphosphate / Q000737:chemistry; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry; D002384:Catalysis; D019281:Dimerization; D004579:Electron Transport; D004926:Escherichia coli / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008968:Molecular Conformation; D010105:Oxygenases / Q000737:chemistry*; D010802:Phylogeny; D011809:Quinones / Q000737:chemistry
D001426:Bacterial Proteins; D011809:Quinones; D006859:Hydrogen; D000255:Adenosine Triphosphate; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010105:Oxygenases