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H + /e − stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes Rate‐dependent changes of the stoichiometry in the cytochrome c oxidase vesicles
Author(s) -
Capitanio N.,
Capitanio G.,
De Nitto E.,
Villani G.,
Papa S.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81029-8
Subject(s) - stoichiometry , cytochrome c oxidase , vesicle , liposome , chemistry , cytochrome , cytochrome c , electron transport complex iv , biophysics , mitochondrion , biochemistry , membrane , enzyme , biology
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.