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

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 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.

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