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• W2024280615 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." @default.
• W2024280615 created "2016-06-24" @default.
• W2024280615 creator A5000952887 @default.
• W2024280615 creator A5058296152 @default.
• W2024280615 date "2005-01-01" @default.
• W2024280615 modified "2023-10-16" @default.
• W2024280615 title "Energy-Converting [NiFe] Hydrogenases: More than Just H₂ Activation" @default.
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• W2024280615 doi "https://doi.org/10.1159/000091557" @default.
• W2024280615 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16645307" @default.
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