Energy-converting [NiFe] hydrogenases: more than just H2 activation

J Mol Microbiol Biotechnol. 2005;10(2-4):92-104. doi: 10.1159/000091557.

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 types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aldehyde Oxidoreductases / metabolism
  • Bacterial Proteins / metabolism*
  • Electron Transport Complex I / metabolism*
  • Energy Transfer*
  • Hydrogen / metabolism*
  • Hydrogenase / metabolism*
  • Multienzyme Complexes / metabolism
  • Oxidation-Reduction
  • Oxidoreductases / metabolism

Substances

  • Bacterial Proteins
  • Multienzyme Complexes
  • Hydrogen
  • Oxidoreductases
  • nickel-iron hydrogenase
  • Hydrogenase
  • Ech hydrogenase
  • Aldehyde Oxidoreductases
  • carbon monoxide dehydrogenase
  • Electron Transport Complex I