Abdolrasulnia R, Wood J L
Biochim Biophys Acta. 1979 Mar 16;567(1):135-43. doi: 10.1016/0005-2744(79)90180-3.
THiocystine (bis-[2-amino-2-carboxyethyl]trisulfide) is a natural substrate for rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1). Analogs of thiocystine were prepared by eliminating the carboxyl or amino group or by lengthening the carbon chain. Of these only homothiocystine (bis-[2-amino-2-carboxypropyl]trisulfide) had appreciable activity as a substrate. At pH 8.6, the optimum for rhodanese, transfer of sulfane sulfur to cyanide in the presence of rhodanese was nonspecific. Only the sulfane sulfur of 35S-labeled thiocystine was transferred to rhodanese. Thus, thiocystine and thiosulfate both produce a rhodanese persulfide as a stable intermediate in sulfur transfer.
硫胱氨酸（双-[2-氨基-2-羧乙基]三硫化物）是硫氰酸酶（硫代硫酸盐：氰化物硫转移酶，EC 2.8.1.1）的天然底物。通过去除羧基或氨基或延长碳链制备了硫胱氨酸类似物。其中只有高硫胱氨酸（双-[2-氨基-2-羧丙基]三硫化物）作为底物具有可观的活性。在pH 8.6（硫氰酸酶的最适pH）下，在硫氰酸酶存在时，次磺酸硫向氰化物的转移是非特异性的。只有35S标记的硫胱氨酸的次磺酸硫转移到了硫氰酸酶上。因此，硫胱氨酸和硫代硫酸盐在硫转移过程中都会产生一种硫氰酸酶过硫化物作为稳定中间体。
