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PMID: 6244543 Published · ppublish English Journal Article

A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 1 ·1980-01-00 ·Pages 196-200

Ludwig B, Schatz G

Abstract

Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC 1.9.3.1) was purified from the cytoplasmic membrane of the bacterium Paracoccus denitrificans. The enzyme contains two heme groups (a and a3) and two copper atoms per minimal unit, oxidizes mammalian cytochrome c at a high rate, and, when incorporated into liposomes, generates an electrochemical proton gradient during cytochrome c oxidation. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis reveals only two subunits of apparent molecular weights 45,000 and 28,000; they appear to correspond to the two largest mitochondrially made subunits of the seven-subunit cytochrome c oxidase isolated from yeast mitochondria. Because of its structural simplicity. Paracoccus cytochrome c oxidase offers new possibilities for exploring the mechanism of cytochrome c oxidase function.

MeSH Terms
Amino Acids/analysis Bacterial Proteins Electron Transport Electron Transport Complex IV/metabolism Lipid Bilayers Macromolecular Substances Mitochondria/enzymology Paracoccus denitrificans/enzymology Uncoupling Agents/pharmacology
Chemicals
Amino Acids Bacterial Proteins Lipid Bilayers Macromolecular Substances Uncoupling Agents Electron Transport Complex IV
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ludwig B
Schatz G
References (28)
28 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.77.1.196
Published
1980-01-00
Pages
196-200
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348235
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.1.196 PMC Full Text View journal details
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