Diphosphatidylglycerol Reactivation of Lipid-Depleted Beef Heart Cytochrome c Oxidase: Effect of Subunit III Removal

Neal C. Robinson, Diane Wiginton

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Beef heart cytochrome c oxidase can be fully delipidated by Triton X-100 using an alkaline pH, high ionic strength incubation followed by glycerol gradient centrifugation at pH 8 in 1% Triton X-100. Unfortunately, this procedure removes not only the 2-3 diphosphati-dylglycerol (DPG) molecules that are tightly bound to each heme aa3 complex, but also removes subunit III. A one-to-one correlation exists between the percent of subunit III removed and the percent of tightly bound DPG extracted, suggesting a possible tight binding of these two molecules. However, based upon regeneration of most of the electron transport activity of the subunit III deficient complex by exogenous DPG, it appears that the functional DPG binding site must be located on a subunit other than subunit III.

Original languageEnglish (US)
Pages (from-to)171-176
Number of pages6
JournalJournal of Inorganic Biochemistry
Volume23
Issue number3-4
DOIs
StatePublished - Jan 1 1985

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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