Alagna L, Hasnain S S, Piggott B, Williams D J
Biochem J. 1984 Jun 1;220(2):591-5. doi: 10.1042/bj2200591.
Preliminary results of an extended X-ray absorption fine structure (e.x.a.f.s.) and X-ray absorption near edge structure study of jack bean urease have recently been reported [Hasnain & Piggott (1983) Biochem. Biophys. Res. Commun. 112, 279]. These results indicate that the environment of the nickel ion in the enzyme is similar to that in the model compounds Ni(L)2(L')1(ClO4)1 (where L is 1-n-propyl-2-alpha-hydroxybenzylbenzimidazole and L' is the deprotonated form) and Ni(HMB)3(Br)2 (where HMB is 2-hydroxymethylbenzimidazole), the closest similarity being with Ni(L)2-(L')1(ClO4)1. A detailed e.x.a.f.s. analysis has now been carried out and the crystal structures of the two model compounds solved. These results are reported here.
刀豆脲酶的扩展X射线吸收精细结构(EXAFS)和X射线吸收近边结构研究的初步结果最近已有报道[哈斯奈因和皮戈特(1983年),《生物化学与生物物理研究通讯》,第112卷,第279页]。这些结果表明,酶中镍离子的环境与模型化合物Ni(L)2(L')1(ClO4)1(其中L为1-正丙基-2-α-羟基苄基苯并咪唑,L'为去质子化形式)和Ni(HMB)3(Br)2(其中HMB为2-羟甲基苯并咪唑)中的环境相似,与Ni(L)2-(L')1(ClO4)1最为相似。现已进行了详细的EXAFS分析,并解析了这两种模型化合物的晶体结构。此处报告这些结果。