Abstract
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.
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