Summary

A 44-kDa c-type cytochrome was purified from membranes of Rhodobacter capsulatus. The cytochrome contained an ascorbate-reducible haem (α-max 556 nm) and a dithionite-reducible haem (α-max 552 nm) and had catalytic properties which indicated that it was a cytochrome c peroxidase. Increased levels of this cytochrome were observed when dimethylsulphoxide was present during phototrophic growth of cells but this was not observed when trimethylamine-N-oxide was present. The results indicate that the 44-kDa cytochrome is probably not directly involved in the dimethylsulphoxide/trimethylamine-N-oxide respiratory pathway of Rhodobacter capsulatus.

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