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PMID: 2454843 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The location of CuA in mammalian cytochrome c oxidase.

FEBS letters ·Vol. 233 ·No. 1 ·1988-06-06 ·Pages 25-30

Rich PR, West IC, Mitchell P

Abstract

Imposition of a protonmotive force across the inner membrane of coupled cyanide-inhibited, beef heart mitochondria by addition of ATP causes reduction of cytochrome c and CuA with concomitant oxidation of haem aA. The data are consistent with previous demonstrations of an intramembrane location of haem aA but further indicate that CuA is very close to the cytosolic surface of the membrane. The implications of this finding for electron transfer route and the site of the proton pumping chemistry are discussed.

MeSH Terms
Adenosine Triphosphate/pharmacology Animals Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone/pharmacology Cattle Copper/analysis,metabolism Cytochrome c Group/metabolism Electron Transport Complex IV/analysis,metabolism Heme/analogs & derivatives,analysis,metabolism Hydrogen-Ion Concentration Intracellular Membranes/analysis Ion Channels Membrane Potentials Mitochondria, Heart/drug effects,enzymology Mitochondria, Liver/drug effects,enzymology Oxidation-Reduction Potassium Cyanide/pharmacology Protons Rats Spectrophotometry
Chemicals
Cytochrome c Group Ion Channels Protons heme a Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone Heme Copper Adenosine Triphosphate Electron Transport Complex IV Potassium Cyanide
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Rich P R
Glynn Research Institute, Bodmin, England.
West I C
Mitchell P
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
DOI
10.1016/0014-5793(88)81349-8
Published
1988-06-06
Pages
25-30
Language
English
Region
England
NLM ID
0155157
Subset
IM
External Links
PubMed source DOI: 10.1016/0014-5793(88)81349-8 View journal details
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