| Literature DB >> 13142 |
Abstract
Rhodanese (thiosulphate:cyanide sulphurtransferase EC.2.8.1.1) was purified 25- to 30-fold from thiosulphate-grown Thiobacillus A2. It exhibited a pH optimum between pH 10-2 and 10-4 and apparent Km values of 0-36 mM-Na2S2O3 and 17 mM-KCN. Ultraviolet spectrophotometry and thin-layer chromatography showed that the enzyme catalysed the reaction of S2O3(2-) with dihydrolipoic acid or dihydrolipoamide, producing alpha-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.Entities:
Mesh:
Substances:
Year: 1976 PMID: 13142 DOI: 10.1099/00221287-97-2-277
Source DB: PubMed Journal: J Gen Microbiol ISSN: 0022-1287