Involvement of phospholipid, biomembrane integrity, and NO peroxidase activity in the NO catabolism by cytochrome c oxidase

Yeong Renn Chen, Chwen Lih Chen, Xiaoping Liu, Guanglong He, Jay L. Zweier

Research output: Contribution to journalArticle

Abstract

The physiological regulation of mitochondrial respiration by NO has been reported to result from the reversible binding of NO to the two-electron reduced binuclear center (Fea32+-CuB1+) of cytochrome c oxidase (CcO). Although the role of CcO and its derived catalytic intermediates in the catabolism of NO has been documented, little has been established for the enzyme in its fully oxidized state (Fea3 3+-CuB2+). We report: (1) CcO, in its fully oxidized state, represents the major component of the mitochondrial electron transport chain for NO consumption as controlled by the binding of NO to its binuclear center. Phospholipid enhances NO consumption by fully oxidized CcO, whereas the consumption of NO is slowed down by membrane structure and membrane potential when CcO is embedded in the phospholipid bilayer. (2) In the presence of H2O2, CcO was shown to serve as a mitochondria-derived NO peroxidase. A CcO-derived protein radical intermediate was induced and involved in the modulation of NO catabolism.

Original languageEnglish (US)
Pages (from-to)200-210
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume439
Issue number2
DOIs
StatePublished - Jul 15 2005
Externally publishedYes

Keywords

  • CcO
  • HO
  • Membrane integrity
  • NO
  • Peroxidase
  • Phospholipid
  • Protein radical
  • SMP

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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