Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH--ubiquinone oxidoreductase (Complex I)

FEBS Lett. 2000 Nov 17;485(1):1-6. doi: 10.1016/s0014-5793(00)02172-4.

Abstract

Hydrogenases have clear evolutionary links to the much more complex NADH-ubiquinone oxidoreductases (Complex I). Certain membrane-bound [NiFe]-hydrogenases presumably pump protons. From a detailed comparison of hydrogenases and Complex I, it is concluded here that the TYKY subunit in these enzymes is a special 2[4Fe-4S] ferredoxin, which functions as the electrical driving unit for a proton pump. The comparison further revealed that the flavodoxin fold from [NiFe]-hydrogenases is presumably conserved in the PSST subunit of Complex I. It is proposed that bovine Complex I and the soluble NAD(+)-reducing hydrogenase from Ralstonia eutropha each contain a second FMN group.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Dimerization
  • Electron Transport Complex I
  • Ferredoxins / chemistry
  • Flavin Mononucleotide / analysis*
  • Hydrogenase / chemistry
  • Iron
  • Molecular Sequence Data
  • NADH, NADPH Oxidoreductases / chemistry*
  • Nickel
  • Proton Pumps / analysis*
  • Sequence Alignment

Substances

  • Ferredoxins
  • Proton Pumps
  • Flavin Mononucleotide
  • Nickel
  • Iron
  • Hydrogenase
  • NADH, NADPH Oxidoreductases
  • Electron Transport Complex I