Silver M, Kelly D P
J Gen Microbiol. 1976 Dec;97(2):277-84. doi: 10.1099/00221287-97-2-277.
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.
从以硫代硫酸盐为生长底物的硫杆菌A2中纯化出的硫氰酸酶(硫代硫酸盐:氰化物硫转移酶,EC.2.8.1.1),纯化倍数达25至30倍。该酶的最适pH值在10.2至10.4之间,其表观Km值分别为0.36 mM的Na2S2O3和17 mM的KCN。紫外分光光度法和薄层色谱法表明,该酶催化S2O3(2-)与二氢硫辛酸或二氢硫辛酰胺反应,生成α-硫辛酸或硫辛酰胺,中间产物为二氢硫辛酸和二氢硫辛酰胺的过硫化物,已通过色谱法得到证实。这是首次证明硫杆菌硫氰酸酶催化的反应可能在硫代硫酸盐通过核心能量守恒途径进行氧化异化作用中具有重要生理意义。