Cytochromes and anaerobic sulfide oxidation in the purple sulfur bacterium Chromatium warmingii.

Two soluble acidic c-type cytochromes--c' and c-552--were isolated by ion exchange chromatography, gel filtration and ammonium sulfate fractionation. Cytochrome c' is a high-spin cytochrome with maxima at 399 nm, 490 nm, and 634 nm in the oxidized form and at 550 nm, 425 nm and a characteristic shoulder at 434 nm in the reduced state. The best purity index obtained (A280/A399) was 0.35. Cytochrome c' is autoxidizable, has a molecular weight of 12000 (estimated by sodium dodecylsulfate electrophoresis), a midpoint redoxpotential of +10 mV and an isoelectric point at pH 4.0. The reduced cytochrome c' reacts with carbon monoxide. The reaction is reversible. Cytochrome c-552 shows maxima at 552 nm, 523 nm and 417 nm in the reduced form and at 408 nm in the oxidized state. The best purity index obtained (A280/A408) was 0.94. Cytochrome c-552 has a molecular weight of 30000 and an isoelectric point between pH 4.3 and 5.0. Chromatium warmingii also contains a membrane-bound cytochrome c-552. During anaerobic sulfide oxidation, elemental sulfur and sulfate were formed at the same time. When all sulfide was consumed by the cells, the remaining intracellular elemental sulfur was further oxidized to sulfate.