Functional binding of cardiolipin to cytochrome c oxidase

Neal C. Robinson

Research output: Contribution to journalArticlepeer-review

213 Scopus citations

Abstract

Bovine cytochrome c oxidase usually contains 3-4 mol of tightly bound cardiolipin per cytochrome aa3 complex. At least two of these cardiolipins are required for full electron transport activity. Without the tightly bound cardiolipin, cytochrome c oxidase has only 40-50% of its original activity when assayed in detergents that support activity, e.g., dodecyl maltoside. By measuring the restoration of electron transport activity, functional binding constants for cardiolipin and a number of cardiolipin analogues have been evaluated (Kd,app=1 μM for cardiolipin). These binding constants agree reasonably well with direct measurement of the binding using [14C]-acetyl-cardiolipin (Kd<0.1 μM) when the enzyme is solubilized with Triton X-100. These data are discussed in relationship to the wealth of data that is known about the association of cardiolipin with cytochrome c oxidase and the other mitochrondrial electron transport complexes and transporters.

Original languageEnglish (US)
Pages (from-to)153-163
Number of pages11
JournalJournal of Bioenergetics and Biomembranes
Volume25
Issue number2
DOIs
StatePublished - Apr 1993

Keywords

  • azido-cardiolipin
  • binding
  • cardiolipin
  • cytochrome c oxidase
  • diphosphatidylglycerol
  • electron transport activity
  • photolabeling
  • spin-labeled cardiolipin
  • synthesis of cardiolipin analogues

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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