Characterization of a new membrane-bound cytochrome c of Rhodopseudomonas capsulata

A cytochrome c (cyt. c) was solubilized with Triton-X-100 and co-purified with cytochrome c oxidase from membranes of chemotrophically grown cells of Rhodopseudomonas capsulata. Cyt. c and cytochrome oxidase were separated on Sephadex G-50 columns. Antibodies against cytochrome c 2 from the same bac...

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Bibliographic Details
Published in:FEBS letters 1983-02, Vol.152 (2), p.251-255
Main Authors: Hüdig, Hendrik, Drews, Gerhart
Format: Article
Language:English
Subjects:
Cell Membrane - metabolism
Cytochrome c
Cytochrome c Group - metabolism
Cytochrome oxidase
Electron Transport
Electron Transport Complex IV - metabolism
Potentiometry
Rhodopseudomonas - metabolism
Rhodopseudomonas capsulata
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Summary:A cytochrome c (cyt. c) was solubilized with Triton-X-100 and co-purified with cytochrome c oxidase from membranes of chemotrophically grown cells of Rhodopseudomonas capsulata. Cyt. c and cytochrome oxidase were separated on Sephadex G-50 columns. Antibodies against cytochrome c 2 from the same bacterium did not cross react with the membrane-bound cyt. c. The IEP of the membrane-bound cyt. c was found to be pH 8.2 the midpoint potential was 234 ± 11 mV at pH 7.0. This cyt. c binds CO. The native cyt. c is a dimer with an apparent M r of 25 000 containing 2 mol heme per mol dimer, which is believed to function as an electron donor for the high-potential cytochrome c oxidase.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(83)80390-1