Flavocytochrome c ‐552, isolated from the photosynthetic purple sulfur bacterium Chromatium vinosum , after linkage to an Affigel 10‐affinity matrix, will bind equine and yeast mitochondrial cytochromes c, C. vinosum cytochrome c ‐550 and cytochrome c 2 from the photosynthetic purple non‐sulfur bacterium Rhodo‐pseudomonas viridis . Similarly, an equine cytochrome c ‐Sepharose 4B affinity column will bind the C. vinosum flavocytochrome c ‐552 and its separated heme‐containing subunit. These results and the correlation between the effect of ionic strength on binding of the flavocytochrome c ‐552 to cytochrome c and on the sulfide:cytochrome c oxidoreductase activity catalyzed by C. vinosum flavocytochrome c ‐552 support the idea of the involvement of an electrostatic complex between the two proteins during sulfide oxidation.
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Davidson et al. (1985) studied this question.
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