光合硫细菌玫瑰色荚硫菌腺苷硫酸还原酶的纯化及性质
Purification and properties of adenylyl sulfate reductase from the phototrophic sulfur bacterium, Thiocapsa roseopersicina.
作者信息
Trüper H G, Rogers L A
出版信息
J Bacteriol. 1971 Dec;108(3):1112-21. doi: 10.1128/jb.108.3.1112-1121.1971.
Abstract
Adenylyl sulfate reductase was purified from Thiocapsa roseopersicina 60- to 80- fold, and the properties were studied. The molecular weight is 180,000. The enzyme contains, per molecule; one flavine group, two heme groups of cytochrome c character, four atoms of nonheme iron, and six labile sulfide groups. Cytochrome c and ferricyanide serve as electron acceptors. With ferricyanide as the electron acceptor, the pH optimum of the enzyme is at 8.0; with cytochrome c, the pH optimum is at 9.0. Of the nucleotides studied, adenosine 5'-monophosphate is most effective. The influence of substrate concentrations on the activity of the enzyme was studied, and the K(m) values for sulfite, adenosine 5'-monophosphate, ferricyanide, and cytochrome c were determined. The properties of the enzyme are compared with those of adenylyl sulfate reductases purified from sulfate-reducing bacteria and thiobacilli.
摘要
腺苷硫酸还原酶从玫瑰色硫杆菌中纯化了60至80倍，并对其性质进行了研究。分子量为180,000。该酶每分子含有一个黄素基团、两个具有细胞色素c特性的血红素基团、四个非血红素铁原子和六个不稳定的硫化物基团。细胞色素c和铁氰化物作为电子受体。以铁氰化物作为电子受体时，该酶的最适pH为8.0；以细胞色素c作为电子受体时，最适pH为9.0。在所研究的核苷酸中，5'-单磷酸腺苷最有效。研究了底物浓度对酶活性的影响，并测定了亚硫酸盐、5'-单磷酸腺苷、铁氰化物和细胞色素c的米氏常数（K(m)）。将该酶的性质与从硫酸盐还原细菌和硫杆菌中纯化的腺苷硫酸还原酶的性质进行了比较。
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