The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases

FEBS Lett. 2000 Aug 11;479(1-2):1-5. doi: 10.1016/s0014-5793(00)01867-6.


The proton-pumping NADH:ubiquinone oxidoreductase, also called complex I, is the first of the respiratory complexes providing the proton motive force which is essential for energy consuming processes like the synthesis of ATP. Homologues of this complex exist in bacteria, archaea, in mitochondria of eukaryotes and in chloroplasts of plants. The bacterial and mitochondrial complexes function as NADH dehydrogenase, while the archaeal complex works as F420H2 dehydrogenase. The electron donor of the cyanobacterial and plastidal complex is not yet known. Despite the different electron input sites, 11 polypeptides constitute the structural framework for proton translocation and quinone binding in the complex of all three domains of life. Six of them are also present in a family of membrane-bound multisubunit [NiFe] hydrogenases. It is discussed that they build a module for electron transfer coupled to proton translocation.

Publication types

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

MeSH terms

  • Archaea / enzymology
  • Archaea / genetics
  • Bacteria / enzymology
  • Bacteria / genetics
  • Chloroplasts / enzymology
  • Electron Transport
  • Electron Transport Complex I
  • Eukaryotic Cells
  • Evolution, Molecular
  • Mitochondria / enzymology
  • NADH, NADPH Oxidoreductases / chemistry*
  • NADH, NADPH Oxidoreductases / genetics
  • NADH, NADPH Oxidoreductases / metabolism*
  • Protein Structure, Quaternary
  • Protons


  • Protons
  • NADH, NADPH Oxidoreductases
  • Electron Transport Complex I