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A thiosulphate-cytochrome c reductase was highly purified from Chlorobium thiosulphatophilum and its properties were studied. The enzyme catalyses reduction with Na 2 S 2 O 3 of c cytochromes, including cytochrome c -551 of the bacterium. Cytochrome c (555, C. thiosulphatophilum ) does not react directly with the enzyme at an appreciable rate but stimulates greatly the reduction by the enzyme of cytochrome c -551 with Na 2 S 2 O 3 . The reduction of c cytochromes catalysed by the enzyme is strongly inhibited by cyanide and sulphite. Cytochrome c (553, C. thiosulphatophilum ), a c -type cytochrome with covalently bound flavin, was found to catalyse reduction with sulphide of c cytochromes, including cytochrome c -555. The reaction is strongly inhibited by cyanide. Cyanide seems to combine strongly with cytochrome c -553 probably at the flavin moiety. Thus, the absorption spectrum attributable to flavin of the haemoprotein is changed on addition of cyanide, and neither the original spectrum nor the activity reappears even after the cyanide-treated cytochrome has been subjected to gel filtration with a Sephadex G-25 column or to isoelectric focusing.

A cytochrome c peroxidase (ferrocytochrome c :H 2 O 2 oxidoreductase, EC 1.11.1.5) was isolated and highly purified from Thiobacillus novellus , and its properties were studied. The enzyme has haem c as the prosthetic group, and shows a peak at 398 nm in the oxidized form and peaks at 415, 520 and 550 nm in the reduced form. It peroxidatically oxidizes the reduced form of cytochrome c (550, Thiobacillus novellus ) and mammalian-type cytochromes c but does not react or reacts very poorly with bacterial c -type cytochromes such as cytochrome c (551, Pseudomonas aeruginosa ), cytochrome c (552, Nitrosomonas europaea ) and cytochrome c (555, Chlorobium thiosulfatophilum ). One mole of the enzyme oxidizes peroxidatically 2450 moles of tuna ferrocytochrome c per min at pH 8.5 and at 18 °C. The peroxidase reaction catalysed by the enzyme is strongly inhibited by cyanide and azide.