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PMID: 6290474 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Proton transport by cytochrome c oxidase from the thermophilic bacterium PS3 reconstituted in liposomes.

The Journal of biological chemistry ·Vol. 257 ·No. 21 ·1982-11-10 ·Pages 12600-4

Sone N, Hinkle PC

Abstract

Cytochrome oxidase from the thermophilic bacterium PS3 which contains three types of polypeptide subunits are reconstituted into liposomes by a freeze-thaw technique. The reconstituted enzyme caused acidification of the medium during cytochrome c oxidation with a stoichiometry of up to 0.8 H+/e. Uptake of K+ ions in the presence of valinomycin occurred with a stoichiometry between 1.5 and 2 K+/e. Dicyclohexylcarbodiimide inhibited the acidification and decreased the stoichiometry of K+ ion uptake to about 1 K+/e. This bacterial oxidase thus appears to be a proton pump with properties similar to the mitochondrial enzyme.

MeSH Terms
Bacteria/enzymology Biological Transport Dicyclohexylcarbodiimide/pharmacology Electron Transport Complex IV/metabolism Hydrogen-Ion Concentration Kinetics Liposomes Potassium/metabolism Temperature
Chemicals
Liposomes Dicyclohexylcarbodiimide Electron Transport Complex IV Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sone N
Hinkle P C
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1982-11-10
Pages
12600-4
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NHLBI NIH HHS · HL-14483 · United States
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