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Fe-only hydrogenases: structure, function and evolution.
- Source :
-
Journal of inorganic biochemistry [J Inorg Biochem] 2002 Jul 25; Vol. 91 (1), pp. 1-8. - Publication Year :
- 2002
-
Abstract
- Hydrogenases are enzymes capable of catalyzing the oxidation of molecular hydrogen or its production from protons and electrons according to the reversible reaction: H(2)<==>2H(+)+2e(-). Most of these enzymes fall into to major classes: NiFe and Fe-only hydrogenases. Extensive spectroscopic, electrochemical and structural studies have shed appreciable light on the catalytic mechanism of hydrogenases. Although evolutionarily unrelated, NiFe and Fe-hydrogenases share a common, unusual feature: an active site low-spin Fe center with CO and CN coordination. We have recently focused our attention on Fe-hydrogenases because from structural studies by us and others, it appears to be a simpler system than the NiFe counterpart. Thus the primary hydrogen binding site has been identified and plausible, electron, proton and hydrogen pathways from and to the buried active site may be proposed from the structural data. The extensive genome sequencing effort currently under way has shown that eukaryotic organisms contain putatively gene coding sequences that display significant homology to Fe-hydrogenases. Here, we summarize the available evidence concerning the mechanism of these enzymes and carry out a structural comparison between Fe-hydrogenases and related proteins of unknown metal content from yeast, plant, worm, insect and mammals.
- Subjects :
- Amino Acid Sequence
Archaeal Proteins chemistry
Archaeal Proteins genetics
Archaeal Proteins metabolism
Bacterial Proteins chemistry
Bacterial Proteins genetics
Bacterial Proteins metabolism
Binding Sites
Electron Transport physiology
Humans
Hydrogenase genetics
Hydrogenase metabolism
Metalloproteins genetics
Metalloproteins metabolism
Models, Molecular
Molecular Sequence Data
Oxidation-Reduction
Protein Structure, Tertiary
Sequence Alignment
Evolution, Molecular
Hydrogen metabolism
Hydrogenase chemistry
Iron chemistry
Metalloproteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0162-0134
- Volume :
- 91
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of inorganic biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 12121756
- Full Text :
- https://doi.org/10.1016/s0162-0134(02)00392-6