Myxothiazol induces H(2)O(2) production from mitochondrial respiratory chain. Academic Article uri icon

Overview

MeSH

  • Animals
  • Electron Transport
  • Male
  • Methacrylates
  • Rats
  • Rats, Sprague-Dawley

MeSH Major

  • Hydrogen Peroxide
  • Mitochondria, Heart
  • Thiazoles

abstract

  • Interruption of electron flow at the quinone-reducing center (Q(i)) of complex III of the mitochondrial respiratory chain results in superoxide production. Unstable semiquinone bound in quinol-oxidizing center (Q(o)) of complex III is thought to be the sole source of electrons for oxygen reduction; however, the unambiguous evidence is lacking. We investigated the effects of complex III inhibitors antimycin, myxothiazol, and stigmatellin on generation of H(2)O(2) in rat heart and brain mitochondria. In the absence of antimycin A, myxothiazol stimulated H(2)O(2) production by mitochondria oxidizing malate, succinate, or alpha-glycerophosphate. Stigmatellin inhibited H(2)O(2) production induced by myxothiazol. Myxothiazol-induced H(2)O(2) production was dependent on the succinate/fumarate ratio but in a manner different from H(2)O(2) generation induced by antimycin A. We conclude that myxothiazol-induced H(2)O(2) originates from a site located in the complex III Q(o) center but different from the site of H(2)O(2) production inducible by antimycin A. Copyright 2001 Academic Press.

publication date

  • March 2, 2001

has subject area

  • Animals
  • Electron Transport
  • Hydrogen Peroxide
  • Male
  • Methacrylates
  • Mitochondria, Heart
  • Rats
  • Rats, Sprague-Dawley
  • Thiazoles

Research

keywords

  • Journal Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1006/bbrc.2001.4409

PubMed ID

  • 11237706

Additional Document Info

start page

  • 645

end page

  • 650

volume

  • 281

number

  • 3