Korsunskiĭ O F, Gogotov I N
Biokhimiia. 1980 Aug;45(8):1488-96.
The purification by affinity chromatography up to homogeneity and the properties of NAD-reductase from purple sulfur bacterium Thiocapsa roseopersicina, strain BBS, are described. The molecular weight of NAD-reductase is about 80000; pI is 3.9. The enzyme consists of two subunits. According to the stabilizing effect of FAD at preparative electrophoresis and the inhibitory effect of atebrine NAD-reductase is a flavoprotein. The bulk of the enzyme (about 75%) is localized in the cell periplasmic space. NAD-reductase is less thermostable and has a lower O2 stability as compared to the NADP-reductase from the same organism. The enzyme is specific to NADH ane catalyzes the menadione-reductase reaction, diaphorase reaction of benzyl viologen and methyl viologen reductions. In the presence of NADH NAD-reductase reduces cytochromes c552 and "c3" from T. roseopersicina and forms a complex with spinach ferredoxin.
本文描述了通过亲和层析法将紫色硫细菌玫瑰色硫囊菌（Thiocapsa roseopersicina）BBS菌株的NAD还原酶纯化至同质的过程及其性质。NAD还原酶的分子量约为80000；等电点为3.9。该酶由两个亚基组成。根据FAD在制备电泳中的稳定作用以及阿的平的抑制作用，NAD还原酶是一种黄素蛋白。大部分酶（约75%）位于细胞周质空间。与来自同一生物体的NADP还原酶相比，NAD还原酶的热稳定性较低，对O2的稳定性也较低。该酶对NADH具有特异性，催化甲萘醌还原酶反应、苄基紫精和甲基紫精还原的双氢酶反应。在NADH存在的情况下，NAD还原酶可还原玫瑰色硫囊菌的细胞色素c552和“c3”，并与菠菜铁氧还蛋白形成复合物。
