H+/e- stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes. Rate-dependent changes of the stoichiometry in the cytochrome c oxidase vesicles

N Capitanio; G Capitanio; E De Nitto; G Villani; S Papa

doi:10.1016/0014-5793(91)81029-8

H+/e- stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes. Rate-dependent changes of the stoichiometry in the cytochrome c oxidase vesicles

FEBS Lett. 1991 Aug 19;288(1-2):179-82. doi: 10.1016/0014-5793(91)81029-8.

Authors

N Capitanio¹, G Capitanio, E De Nitto, G Villani, S Papa

Affiliation

¹ Institute of Medical Biochemistry and Chemistry, Faculty of Medicine, University of Bari, Italy.

PMID: 1652471
DOI: 10.1016/0014-5793(91)81029-8

Abstract

The H+/e- stoichiometry of protonmotive cytochrome c oxidase, isolated from bovine heart mitochondria and reconstituted in liposomes, has been determined by making use of direct spectrophotometric measurements of the initial rates of e- flow and H+ translocation. It is shown that the ----H+/e- ratio for redox-linked proton ejection by the oxidase varies from around 0 to a maximum of 1 as a function of the rate of overall electron flow in the complex.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Ascorbic Acid / metabolism
Cattle
Electron Transport / physiology*
Electron Transport Complex IV / metabolism*
Hydrogen / metabolism*
Hydrogen-Ion Concentration
Kinetics
Liposomes / metabolism
Mitochondria, Heart / metabolism*
NADH Dehydrogenase / metabolism
Spectrophotometry

Substances

Liposomes
Hydrogen
NADH Dehydrogenase
Electron Transport Complex IV
Ascorbic Acid