Kim J H, Akagi J M
J Bacteriol. 1985 Aug;163(2):472-5. doi: 10.1128/jb.163.2.472-475.1985.
A trithionate reductase system was isolated and purified from extracts of Desulfovibrio vulgaris. This system reduced trithionate to thiosulfate and consisted of two proteins. One was bisulfite reductase, an enzyme that reduces bisulfite to trithionate, and the second component was designated TR-1. Both enzymes were required to reduce trithionate to thiosulfate. Flavodoxin and cytochrome c3 from D. vulgaris were tested for their ability to function as electron carriers during trithionate reduction. When molecular hydrogen was the source of electrons for the reduction, both flavodoxin and cytochrome c3 were required. In contrast, when the pyruvate phosphoroclastic system was the reductant, flavodoxin alone participated as the electron carrier. The results indicate that flavodoxin, but not cytochrome c3, interacted with the trithionate reductase system. The cytochrome in the hydrogenase-linked assay functioned as an electron carrier between hydrogenase and flavodoxin.
从普通脱硫弧菌提取物中分离并纯化出一种连三硫酸盐还原酶系统。该系统将连三硫酸盐还原为硫代硫酸盐，由两种蛋白质组成。一种是亚硫酸氢盐还原酶，可将亚硫酸氢盐还原为连三硫酸盐，第二种成分被命名为TR - 1。两种酶都需要将连三硫酸盐还原为硫代硫酸盐。对来自普通脱硫弧菌的黄素氧还蛋白和细胞色素c3在连三硫酸盐还原过程中作为电子载体的功能进行了测试。当分子氢作为还原反应的电子来源时，黄素氧还蛋白和细胞色素c3都需要。相反，当丙酮酸磷酸裂解系统作为还原剂时，只有黄素氧还蛋白作为电子载体参与。结果表明，与连三硫酸盐还原酶系统相互作用的是黄素氧还蛋白，而非细胞色素c3。在与氢化酶相关的测定中，细胞色素作为氢化酶和黄素氧还蛋白之间的电子载体发挥作用。
