Nishida H, Inaka K, Miki K
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
FEBS Lett. 1995 Mar 13;361(1):97-100. doi: 10.1016/0014-5793(95)00161-2.
The structure of NADH-cytochrome b5 reductase from pig liver microsomes has been refined to a crystallographic R factor of 0.223 at 2.4 A resolution. A structural comparison between the flavin-binding beta barrel domain of NADH-cytochrome b5 reductase and those of the other flavin-dependent reductases, ferredoxin-NADP+ reductase, phthalate dioxygenase reductase and nitrate reductase, indicated that the overall barrel foldings are similar to each other and that the specific arrangement of three amino acid residues (Arg, Tyr and Ser/Thr) is usually necessary for flavin-binding. These conserved residues overlap each other in their three-dimensional structures and stabilize the flavin-binding site in the four flavin-dependent reductases.
猪肝微粒体中NADH-细胞色素b5还原酶的结构已被精修至2.4埃分辨率下晶体学R因子为0.223。对NADH-细胞色素b5还原酶的黄素结合β桶结构域与其他黄素依赖性还原酶（铁氧化还原蛋白-NADP+还原酶、邻苯二甲酸双加氧酶还原酶和硝酸还原酶）的结构比较表明，总体桶状折叠彼此相似，并且三个氨基酸残基（精氨酸、酪氨酸和丝氨酸/苏氨酸）的特定排列通常是黄素结合所必需的。这些保守残基在其三维结构中相互重叠，并稳定了四种黄素依赖性还原酶中的黄素结合位点。
