Decreased affinity for oxygen of cytochrome-c oxidase in Leigh syndrome caused by SURF1 mutations

Am J Physiol Cell Physiol. 2004 Nov;287(5):C1384-8. doi: 10.1152/ajpcell.00286.2004. Epub 2004 Jul 21.

Abstract

Mutations in the gene SURF1 prevent synthesis of cytochrome-c oxidase (COX)-specific assembly protein and result in a fatal neurological disorder, Leigh syndrome. Because this severe COX deficiency presents with barely detectable changes of cellular respiratory rates under normoxic conditions, we analyzed the respiratory response to low oxygen in cultured fibroblasts harboring SURF1 mutations with high-resolution respirometry. The oxygen kinetics was quantified by the partial pressure of oxygen (PO2) at half-maximal respiration rate (P50) in intact coupled cells and in digitonin-permeabilized uncoupled cells. In both cases, the P50 in patients was elevated 2.1- and 3.3-fold, respectively, indicating decreased affinity of COX for oxygen. These results suggest that at physiologically low intracellular PO2, the depressed oxygen affinity may lead in vivo to limitations of respiration, resulting in impaired energy provision in Leigh syndrome patients.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • Cytochrome-c Oxidase Deficiency / genetics
  • Cytochrome-c Oxidase Deficiency / metabolism
  • Cytochrome-c Oxidase Deficiency / physiopathology
  • Electron Transport Complex IV / metabolism*
  • Fibroblasts / metabolism*
  • Humans
  • Leigh Disease / genetics
  • Leigh Disease / metabolism
  • Leigh Disease / physiopathology*
  • Membrane Proteins
  • Mitochondrial Proteins
  • Mutation
  • Oxygen / metabolism*
  • Oxygen Consumption / physiology*
  • Proteins / genetics*

Substances

  • Membrane Proteins
  • Mitochondrial Proteins
  • Proteins
  • Surf-1 protein
  • Electron Transport Complex IV
  • Oxygen