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
[41]   Protein targeting by the bacterial twin-arginine translocation (Tat) pathway [J].
Berks, BC ;
Palmer, T ;
Sargent, F .
CURRENT OPINION IN MICROBIOLOGY, 2005, 8 (02) :174-181
[42]   The Tat protein export pathway [J].
Berks, BC ;
Sargent, F ;
Palmer, T .
MOLECULAR MICROBIOLOGY, 2000, 35 (02) :260-274
[43]   The Tat protein translocation pathway and its role in microbial physiology [J].
Berks, BC ;
Palmer, T ;
Sargent, F .
ADVANCES IN MICROBIAL PHYSIOLOGY, VOL 47, 2003, 47 :187-254
[44]   ACTIVATION, REDUCTION AND PROTON - DEUTERIUM-EXCHANGE REACTION OF THE PERIPLASMIC HYDROGENASE FROM DESULFAVIBRIO-GIGAS IN RELATION WITH THE ROLE OF CYTOCHROME C-3 [J].
BERLIER, YM ;
FAUQUE, G ;
LESPINAT, PA ;
LEGALL, J .
FEBS LETTERS, 1982, 140 (02) :185-188
[45]   The H2 sensor of Ralstonia eutropha -: Biochemical characteristics, spectroscopic properties, and its interaction with a histidine protein kinase [J].
Bernhard, M ;
Buhrke, T ;
Bleijlevens, B ;
De Lacey, AL ;
Fernandez, VM ;
Albracht, SPJ ;
Friedrich, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (19) :15592-15597
[46]   Ralstonia eutropha TF93 is blocked in tat-mediated protein export [J].
Bernhard, M ;
Friedrich, B ;
Siddiqui, RA .
JOURNAL OF BACTERIOLOGY, 2000, 182 (03) :581-588
[47]   Thermotoga maritima IscU.: Structural characterization and dynamics of a new class of metallochaperone [J].
Bertini, I ;
Cowan, JA ;
Del Bianco, C ;
Luchinat, C ;
Mansy, SS .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 331 (04) :907-924
[48]   Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold [J].
Bilder, PW ;
Ding, H ;
Newcomer, ME .
BIOCHEMISTRY, 2004, 43 (01) :133-139
[49]   Conversion of the central [4Fe-4S] cluster into a [3Fe-4S] cluster leads to reduced hydrogen-uptake activity of the F420-reducing hydrogenase of Methanococcus voltae [J].
Bingemann, R ;
Klein, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (22) :6612-6618
[50]   SEQUENCES AND CHARACTERIZATION OF HUPU AND HUPV GENES OF BRADYRHIZOBIUM-JAPONICUM ENCODING A POSSIBLE NICKEL-SENSING COMPLEX INVOLVED IN HYDROGENASE EXPRESSION [J].
BLACK, LK ;
FU, CL ;
MAIER, RJ .
JOURNAL OF BACTERIOLOGY, 1994, 176 (22) :7102-7106