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PMID: 201286 Published · ppublish English Comparative Study Journal Article

The mechanism of energy conservation and transduction by mitochondrial cytochrome c oxidase.

Biochimica et biophysica acta ·Vol. 462 ·No. 2 ·1977-11-17 ·Pages 347-61

Wikström MK, Saari HT

Abstract

Oxidation of ferrocytochrome c by molecular oxygen catalysed by cytochrome c oxidase (cytochrome aa3) is coupled to translocation of H+ ions across the mitochondrial membrane. The proton pump is an intrinsic property of the cytochrome c oxidase complex as revealed by studies with phospholipid vesicles inlayed with the purified enzyme. As the conformation of cytochrome aa3 is specifically sensitive to the electrochemical proton gradient across the mitochondrial membrane, it is likely that redox energy is primarily conserved as a conformational "strain" in the cytochrome aa3 complex, followed by relaxation linked to proton translocation. Similar principles of energy conservation and transduction may apply on other respiratory chain complexes and on mitochondrial ATP synthase.

MeSH Terms
Animals Biological Transport, Active Cattle Cytochrome c Group/metabolism Electron Transport Complex IV/metabolism Energy Metabolism Membranes/metabolism Mitochondria, Heart/metabolism Mitochondria, Liver/enzymology Molecular Conformation Oxidation-Reduction Protons Rats
Chemicals
Cytochrome c Group Protons Electron Transport Complex IV
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wikström M K
Saari H T
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1977-11-17
Pages
347-61
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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