Occurrence, classification, and biological function of hydrogenases: An overview

被引:1230
作者
Vignais, Paulette M.
Billoud, Bernard
机构
[1] Inst Rech & TEchnol & Sci Vivant, UMR CEA CNRS UJF 5092, CEA, Lab Biochem & Biophys Syst Integres, F-38054 Grenoble 9, France
[2] Atelier Bioinformat Univ Pierre & Marie Curie, F-75005 Paris, France
关键词
D O I
10.1021/cr050196r
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The phylogenetic analyses of the biological function of hydrogenases have led to the identification of several phylogenetically distinct groups and subgroups that form the basis of coherent system of classification. Hydrgeneses are a structurally and functionally diverse group of enzymes and efforts have been made to augment them. This showed the presence of such enzymes in a variety of organisms including pathogens and of multiple hydrogenases. The roles of such enzymes and their biosynthesis and activity can be derived from its postgenomic analysis. Hydrogenases' main role is the oxidation of H2 or the reduction of protons, coupled to energy-conserving electron-transfer chain reactions. This permits energy to be obtained from H2 or from the oxidation of substrates of lower potential. They are restricted to the prokaryotes but nevertheless widely distributed. The biological production of H2 has been stimulated by interests in finding alternatives in fossil fuels. Structural studies of hydrogenases will be relevant in directing protein engineering. Also of relevance is the investigation of H2 metabolism and regulation for engineering microorganisms at the cellular level to maximize H2 production. Many of the so-far uncultivated species will then contain hydrogenases.
引用
收藏
页码:4206 / 4272
页数:67
相关论文
共 619 条
[1]   Iron-sulfur cluster biogenesis in chloroplasts. Involvement of the scaffold protein CpIscA [J].
Abdel-Ghany, SE ;
Ye, H ;
Garifullina, GF ;
Zhang, LH ;
Pilon- Smits, EAH ;
Pilon, M .
PLANT PHYSIOLOGY, 2005, 138 (01) :161-172
[2]   The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria [J].
Adam, AC ;
Bornhövd, C ;
Prokisch, H ;
Neupert, W ;
Hell, K .
EMBO JOURNAL, 2006, 25 (01) :174-183
[3]   Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus [J].
Adams, MWW ;
Holden, JF ;
Menon, AL ;
Schut, GJ ;
Grunden, AM ;
Hou, C ;
Hutchins, AM ;
Jenney, FE ;
Kim, C ;
Ma, KS ;
Pan, GL ;
Roy, R ;
Sapra, R ;
Story, SV ;
Verhagen, MFJM .
JOURNAL OF BACTERIOLOGY, 2001, 183 (02) :716-724
[4]   THE STRUCTURE AND MECHANISM OF IRON-HYDROGENASES [J].
ADAMS, MWW .
BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1020 (02) :115-145
[5]   Regulation of the synthesis of H2-forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of HmdII and HmdIII in Methanothermobacter marburgensis [J].
Afting, C ;
Kremmer, E ;
Brucker, C ;
Hochheimer, A ;
Thauer, RK .
ARCHIVES OF MICROBIOLOGY, 2000, 174 (04) :225-232
[6]  
AFTING C, 2000, THESIS PHILIPPS U MA
[7]   Modular organization and identification of a mononuclear iron-binding site within the NifU protein [J].
Agar, JN ;
Yuvaniyama, P ;
JAck, RF ;
Cash, VL ;
Smith, AD ;
Dean, DR ;
Johnson, MK .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2000, 5 (02) :167-177
[8]   IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU [J].
Agar, JN ;
Krebs, C ;
Frazzon, J ;
Huynh, BH ;
Dean, DR ;
Johnson, MK .
BIOCHEMISTRY, 2000, 39 (27) :7856-7862
[9]   A hydrogenosome with a genome [J].
Akhmanova, A ;
Voncken, F ;
van Alen, T ;
van Hoek, A ;
Boxma, B ;
Vogels, G ;
Veenhuiss, M ;
Hackstein, JHP .
NATURE, 1998, 396 (6711) :527-528
[10]   Photobiological hydrogen production: photochemical efficiency and bioreactor design [J].
Akkerman, I ;
Janssen, M ;
Rocha, J ;
Wijffels, RH .
INTERNATIONAL JOURNAL OF HYDROGEN ENERGY, 2002, 27 (11-12) :1195-1208