Oxidatively damaged proteins of heart mitochondrial electron transport complexes

K. B. Choksi, W. H. Boylston, J. P. Rabek, W. R. Widger, John Papaconstantinou

Research output: Contribution to journalArticle

146 Scopus citations

Abstract

Protein modifications, such as carbonylation, nitration and formation of lipid peroxidation adducts, e.g. 4-hydroxynonenal (HNE), are products of oxidative damage attributed to reactive oxygen species (ROS). The mitochondrial respiratory chain Complexes I and III have been shown to be a major source of ROS in vitro. Additionally, modifications of the respiratory chain Complexes (I-V) by nitration, carbonylation and HNE adduct decrease their enzymatic activity in vitro. However, modification of these respiratory chain complex proteins due to in vivo basal level ROS generation has not been investigated. In this study, we show a basal level of oxidative damage to specific proteins of adult bovine heart submitochondrial particle (SMP) complexes, and find that most of these proteins are localized in the mitochondrial matrix. We postulate that electron leakage from respiratory chain complexes and subsequent ROS formation may cause damage to specific complex subunits and contribute to long-term accumulation of mitochondrial dysfunction.

Original languageEnglish (US)
Pages (from-to)95-101
Number of pages7
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Volume1688
Issue number2
DOIs
StatePublished - Mar 2 2004

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Keywords

  • 4-hydroxynonenal
  • Carbonylation
  • Lipid peroxidation adduct
  • Mitochondrial dysfunction
  • Nitration
  • Oxidative stress

ASJC Scopus subject areas

  • Molecular Biology
  • Molecular Medicine
  • Biophysics

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