Abstract:
: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 c2 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 Mr of 25000 containing 2 mol heme per mol dimer, which is believed to function as an electron donor for the high-potential cytochrome c oxidase.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hüdig H,Drews Gdoi
10.1016/0014-5793(83)80390-1subject
Has Abstractpub_date
1983-02-21 00:00:00pages
251-5issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(83)80390-1journal_volume
152pub_type
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