Action of bovine serum albumin on cytochrome c oxidase activity and proton pumping: A role for fatty acids in enzyme function?

Martyn Sharpe, Ivano Perin, Peter Nicholls

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Bovine serum albumin (BSA) at micromolar concentrations causes a red shift of the Sorer band of bovine cytochrome c oxidase with a slow biphasic time course. It also inhibits the turnover of detergent-isolated enzyme in a similarly slow manner; the progress of this inhibition is halted by palmitate and other fatty acids. The inhibitory bovine serum albumin effect may involve fatty acid depletion from the enzyme. Respiration by cytochrome c oxidase vesicles (proteoliposomes) in the presence of ionophores (uncontrolled) shows only a small inhibition by BSA but preincubation of such vesicles with BSA induces a loss of proton pumping activity. After incubation of BSA-depleted proteoliposomes in the presence of reductant with combinations of fatty acids, pumping activity can be fully restored, suggesting a supportive or even essential role of endogenous fatty acids in H+ translocation by this membranous enzyme.

Original languageEnglish (US)
Pages (from-to)134-138
Number of pages5
JournalFEBS Letters
Volume391
Issue number1-2
DOIs
StatePublished - Aug 5 1996

Keywords

  • Bovine serum albumin
  • Cytochrome c oxidase
  • Fatty acids
  • Oleate
  • Palmitate
  • Proteoliposomes
  • Proton pumping
  • Respiratory control
  • Spectral change

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Action of bovine serum albumin on cytochrome c oxidase activity and proton pumping: A role for fatty acids in enzyme function?'. Together they form a unique fingerprint.

Cite this