Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex

J Biol Chem. 2001 Sep 21;276(38):35231-4. doi: 10.1074/jbc.C100365200. Epub 2001 Jul 31.

Abstract

Bifurcated electron flow to high potential "Rieske" iron-sulfur cluster and low potential heme b(L) is crucial for respiratory energy conservation by the cytochrome bc(1) complex. The chemistry of ubiquinol oxidation has to ensure the thermodynamically unfavorable electron transfer to heme b(L). To resolve a central controversy about the number of ubiquinol molecules involved in this reaction, we used high resolution magic-angle-spinning nuclear magnetic resonance experiments to show that two out of three n-decyl-ubiquinones bind at the ubiquinol oxidation center of the complex. This substantiates a proposed mechanism in which a charge transfer between a ubiquinol/ubiquinone pair explains the bifurcation of electron flow.

Publication types

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

MeSH terms

  • Animals
  • Cattle
  • Electron Transport Complex III / metabolism*
  • Mitochondria / enzymology*
  • Protein Binding
  • Substrate Specificity
  • Ubiquinone / metabolism*

Substances

  • Ubiquinone
  • Electron Transport Complex III