Specific arrangement of three amino acid residues for flavin‐binding barrel structures in NADH‐cytochrome b 5 reductase and the other flavin‐dependent reductases

FEBS Letters

Inaka, Koji¹  Nishida, Hirokazu¹  Miki, Kunio² 

[1] Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 227, Japan;Department of Chemistry, Faculty of Science, Kyoto University, Sakyo-ku, Kyoto 606-01, Japan

关键词: NADH-cytochrome b 5 reductase;    Flavin-dependent reductase;    Flavoprotein;    Electron transfer;    X-ray crystallography;    FAD;    flavin adenine dinucleotide;    NADPH;    nicotinamide adenine dinucleotide phosphate;    NADH;    nicotinamide adenine dinucleotide;    FMN;    flavin mononucleotide;    b5R;    NADH-cytochrome b 5 reductase;    FNR;    ferredoxin-NADP+ reductase;    PDR;    phthalate dioxygenase reductase;    NR;    nitrate reductase;   

DOI  :  10.1016/0014-5793(95)00161-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of NADH-cytochrome b ₅ reductase from pig liver microsomes has been refined to a crystallographic R factor of 0.223 at 2.4 Å resolution. A structural comparison between the flavin-binding β barrel domain of NADH-cytochrome b ₅ 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.

【 授权许可】

Unknown