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- Title
Energy-converting [NiFe] hydrogenases: more than just H2 activation.
- Authors
Hedderich, Reiner; Forzi, Lucia
- Abstract
The well-characterized [NiFe] hydrogenases have a key function in the H2 metabolism of various microorganisms. A subfamily of the [NiFe] hydrogenases with unique properties has recently been identified. The six conserved subunits that build the core of these membrane-bound hydrogenases share sequence similarity with subunits that form the catalytic core of energy-conserving NADH:quinone oxidoreductases (complex I). The physiological role of some of these hydrogenases is to catalyze the reduction of H+ with electrons derived from reduced ferredoxins or polyferredoxins. This exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation. Other members of this hydrogenase subfamily mainly function in providing the cell with reduced ferredoxin using H2 as electron donor in a reaction driven by reverse electron transport. These hydrogenases have therefore been designated as energy-converting [NiFe] hydrogenases.
- Publication
Journal of molecular microbiology and biotechnology, 2005, Vol 10, Issue 2-4, p92
- ISSN
1464-1801
- Publication type
Journal Article
- DOI
10.1159/000091557