Jarabak R, Westley J
J Biol Chem. 1986 Aug 15;261(23):10793-6.
Kinetic studies of the serum albumin-catalyzed reaction of cyanide with colloidal elemental sulfur have been carried out to elucidate the formal mechanism of this reaction. The results indicate that one of the several sulfur-binding sites on the protein molecule is involved in a single displacement catalytic cycle in the presence of cyanide. At high velocities the rate of thiocyanate production is limited by an albumin-independent second order process which produces the form of sulfur that serves as substrate. The catalyzed reaction is also subject to substrate inhibition at high colloidal sulfur concentrations.
已开展血清白蛋白催化氰化物与胶态元素硫反应的动力学研究,以阐明该反应的形式机制。结果表明,在氰化物存在的情况下,蛋白质分子上几个硫结合位点之一参与了单置换催化循环。在高反应速率下,硫氰酸盐的生成速率受一个与白蛋白无关的二级过程限制,该过程产生用作底物的硫的形式。在高胶态硫浓度下,催化反应也会受到底物抑制。