期刊
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY
卷 10, 期 2-4, 页码 92-104出版社
KARGER
DOI: 10.1159/000091557
关键词
hydrogen; [NiFe] hydrogenases; NADH : quinone oxidoreductase; complex I; methanogenic archaea; carbon monoxide dehydrogenase; iron-sulfur proteins
The well-characterized [NiFe] hydrogenases have a key function in the H-2 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 1). 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 H-2 as electron donor in a reaction driven by reverse electron transport. These hydrogenases have therefore been designated as energy-converting [NiFe] hydrogenases. Copyright (c) 2005 S. Karger AG, Basel.
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