Journal of Bioenergetics and Biomembranes

, Volume 25, Issue 4, pp 331–337

Attempts to define distinct parts of NADH: Ubiquinone oxidoreductase (complex I)

Authors

  • Thorsten Friedrich
    • Institut für BiochemieHeinrich-Heine-Universität Düsseldorf
  • Uwe Weidner
    • Institut für BiochemieHeinrich-Heine-Universität Düsseldorf
  • Uwe Nehls
    • Institut für BiochemieHeinrich-Heine-Universität Düsseldorf
  • Wolfgang Fecke
    • Institut für BiochemieHeinrich-Heine-Universität Düsseldorf
  • Regina Schneider
    • Institut für BiochemieHeinrich-Heine-Universität Düsseldorf
  • Hanns Weiss
    • Institut für BiochemieHeinrich-Heine-Universität Düsseldorf
Minireview

DOI: 10.1007/BF00762458

Cite this article as:
Friedrich, T., Weidner, U., Nehls, U. et al. J Bioenerg Biomembr (1993) 25: 331. doi:10.1007/BF00762458

Abstract

The NADH:ubiquinone oxidoreductase (complex I) is made up of a peripheral part and a membrane part. The two parts are arranged perpendicular to each other and give the complex an unusual L-shaped structure. The peripheral part protrudes into the matrix space and constitutes the proximal segment of the electron pathway with the NADH-binding site, the FMN and at least three iron-sulfur clusters. The membrane part constitutes the distal segment of the electron pathway with at least one iron-sulfur cluster and the ubiquinone-binding site. Both parts are assembled separately and relationships of the major structural modules of the two parts with different bacterial enzymes suggest, that both parts also emerged independently in evolution. This assumption is further supported by the conserved order of bacterial complex I genes, which correlates with the topological arrangement of the corresponding subunits in the two parts of complex I.

Key words

NADH:ubiquinone oxidoreductasecomplex Iiron-sulfur clusterassemblygene disruptionNeurospora crassaEscherichia coli

Copyright information

© Plenum Publishing Corporation 1993