Summary: Rhodanese (thiosulphate: cyanide sulphurtransferase EC. was purified 25- to 30-fold from thiosulphate-grown 2. It exhibited a pH optimum between pH 10·2 and 10·4 and apparent values of 0·36 m-NaSO and 17 m-KCN. Ultraviolet spectrophotometry and thin-layer chromatography showed that the enzyme catalysed the reaction of SO with dihydrolipoic acid or dihydrolipoamide, producing α-lipoate or lipoamide, with the intermediate production of the persulphides of dihydrolipoate and dihydrolipoamide, which were demonstrated chromatographically. This is the first demonstration of catalysis by a thiobacillus rhodanese of reactions which are likely to be physiologically important in the oxidative dissimilation of thiosulphate by a central energy-conserving pathway.


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