The basal proton conductance of mitochondria depends on adenine nucleotide translocase content

Biochem J. 2005 Dec 1;392(Pt 2):353-62. doi: 10.1042/BJ20050890.


The basal proton conductance of mitochondria causes mild uncoupling and may be an important contributor to metabolic rate. The molecular nature of the proton-conductance pathway is unknown. We show that the proton conductance of muscle mitochondria from mice in which isoform 1 of the adenine nucleotide translocase has been ablated is half that of wild-type controls. Overexpression of the adenine nucleotide translocase encoded by the stress-sensitive B gene in Drosophila mitochondria increases proton conductance, and underexpression decreases it, even when the carrier is fully inhibited using carboxyatractylate. We conclude that half to two-thirds of the basal proton conductance of mitochondria is catalysed by the adenine nucleotide carrier, independently of its ATP/ADP exchange or fatty-acid-dependent proton-leak functions.

Publication types

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

MeSH terms

  • Animals
  • Cattle
  • Cell Respiration
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / enzymology
  • Drosophila melanogaster / genetics
  • Female
  • Gene Expression Regulation, Enzymologic
  • Horses
  • Male
  • Membrane Potentials
  • Mice
  • Mice, Knockout
  • Mitochondria / enzymology
  • Mitochondria / metabolism*
  • Mitochondrial ADP, ATP Translocases / deficiency
  • Mitochondrial ADP, ATP Translocases / genetics
  • Mitochondrial ADP, ATP Translocases / metabolism*
  • Phospholipids / metabolism
  • Protein Binding
  • Protons*
  • Rabbits
  • Rats
  • Swine


  • Drosophila Proteins
  • Phospholipids
  • Protons
  • sesB protein, Drosophila
  • Mitochondrial ADP, ATP Translocases