Aketagawa J, Kobayashi K, Ishimoto M
J Biochem. 1985 Apr;97(4):1025-32. doi: 10.1093/oxfordjournals.jbchem.a135144.
Thiosulfate reductase was purified to an almost homogeneous state from Desulfovibrio vulgaris, strain Miyazaki F, by ammonium sulfate precipitation, chromatography on DEAE-Toyopearl, Ultrogel AcA 34, and hydroxylapatite, and disc electrophoresis. The specific activity was increased 580-fold over the crude extract. The molecular weight was determined by gel filtration to be 85,000-89,000, differing from those reported for thiosulfate reductases from other Desulfovibrio strains. The enzyme had no subunit structure. When coupled with hydrogenase and methyl viologen, it stoichiometrically reduced thiosulfate to sulfite and sulfide with consumption of hydrogen. It did not reduce sulfite or trithionate. Cytochrome c3 was active as an electron donor. More than 0.75 mM thiosulfate inhibited the enzyme activity. o-Phenanthroline and 2,2'-bipyridine inhibited the enzyme and ferrous ion stimulated the reaction.
通过硫酸铵沉淀、DEAE - 东洋珠层析、Ultrogel AcA 34层析、羟基磷灰石层析及圆盘电泳，从普通脱硫弧菌宫崎F菌株中纯化出了几乎呈均一状态的硫代硫酸盐还原酶。其比活性相较于粗提物提高了580倍。通过凝胶过滤测定其分子量为85,000 - 89,000，这与报道的其他脱硫弧菌菌株的硫代硫酸盐还原酶的分子量不同。该酶没有亚基结构。当与氢化酶和甲基紫精偶联时，它能化学计量地将硫代硫酸盐还原为亚硫酸盐和硫化物，并消耗氢气。它不能还原亚硫酸盐或连三硫酸盐。细胞色素c3作为电子供体具有活性。超过0.75 mM的硫代硫酸盐会抑制酶活性。邻菲罗啉和2,2'-联吡啶会抑制该酶，而亚铁离子会刺激该反应。
