1887

Abstract

Sulphite: cytochrome oxidoreductase (sulphite dehydrogenase) was purified 2000-fold from (A2). The enzyme monomer had a molecular weight of 44000 and a pI value of 4·5 α 0·3. Cytochrome was intimately associated with the enzyme: separation of the two greatly decreased sulphite dehydrogenase activity, which was not restored by remixing them. The enzyme had a pH optimum around pH 8·0, exhibited a of 14 µ for sulphite, and was inhibited noncompetitively by phosphate, with a value of 12 m. It was also inhibited by -hydroxymercuribenzoate and cyanide. Its involvement in the oxidation of thiosulphate in is discussed.

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/content/journal/micro/10.1099/00221287-130-7-1683
1984-07-01
2021-08-03
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