Details

Autor(en) / Beteiligte

• Hedderich, Reiner
• Forzi, Lucia

Titel

Energy-Converting [NiFe] Hydrogenases: More than Just H2 Activation

Ist Teil von

• Journal of molecular microbiology and biotechnology, 2006-04, Vol.10 (2-4), p.92-104

Ort / Verlag

Basel, Switzerland: S. Karger AG

Erscheinungsjahr

2006

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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.