The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.
Open accessAbstract
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.
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Cites
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Capaldi, R., & Vanderkooi, G. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.4.930 · Cited by 498
A method for the simultaneous quantitative estimation of cytochromes a, b, c1, and c in mitochondria
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Cytochrome c Oxidase from Bakers' Yeast
Mason, T. L., Poyton, R. O., Wharton, D. C., & Schatz, G. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44305-6 · Cited by 331
Self-citationProton-pumping cytochrome c oxidase
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Cited by
The Endosymbiont Hypothesis Revisited
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NADH dehydrogenases: from basic science to biomedicine
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Metadata
- Authors
- Ludwig, B., & Schatz, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1980-01
- Volume
- 77
- Issue
- 1
- Pages
- 196-200
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2091263922
- Cited by
- 256
- References
- 15
- FWCI
- 24.76
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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