Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria

J Bioenerg Biomembr. 2008 Oct;40(5):411-7. doi: 10.1007/s10863-008-9168-4. Epub 2008 Oct 7.

Abstract

Accumulating evidence indicates that the enzymes involved in mitochondrial oxidative phosphorylation (OXPHOS) are co-assembled into higher-ordered supercomplexes within the mitochondrial inner membrane. This review will focus largely on the OXPHOS supercomplexes of the yeast Saccharomyces cerevisiae. The recent evidence to indicate that diversity in the populations of the cytochrome bc (1)-COX supercomplexes exist shall be outlined. In addition, the existence of dimeric/oligomeric F(1)F(o)-ATP synthase complexes and their proposed role in establishment of the cristae architecture of the inner mitochondrial membrane shall also be discussed.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Electron Transport Chain Complex Proteins / chemistry*
  • Electron Transport Chain Complex Proteins / metabolism*
  • Electron Transport Complex I / chemistry
  • Electron Transport Complex I / metabolism
  • Electron Transport Complex III / chemistry
  • Electron Transport Complex III / metabolism
  • Electron Transport Complex IV / chemistry
  • Electron Transport Complex IV / metabolism
  • Intracellular Membranes / enzymology
  • Mitochondria / enzymology*
  • Mitochondrial Proton-Translocating ATPases / chemistry
  • Mitochondrial Proton-Translocating ATPases / metabolism
  • Models, Biological
  • Models, Molecular
  • Oxidative Phosphorylation*
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Electron Transport Chain Complex Proteins
  • Electron Transport Complex IV
  • Mitochondrial Proton-Translocating ATPases
  • Electron Transport Complex I
  • Electron Transport Complex III