Nitrate reductase structure, function and regulation: Bridging the gap between biochemistry and physiology

被引：562

作者：

Campbell, WH ^{[1
]}

机构：

[1] Michigan Technol Univ, Phytotechnol Res Ctr, Houghton, MI 49931 USA

[2] Michigan Technol Univ, Dept Biol Sci, Houghton, MI 49931 USA

来源：

ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY | 1999年 / 50卷

关键词：

enzymology; 3-D structure; site-directed mutagenesis; molybdopterin cofactor; regulation; protein phosphorylation; 14-3-3 binding protein;

D O I：

10.1146/annurev.arplant.50.1.277

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nitrate reductase (NR; EC 1.6.6.1-3) catalyzes NAD(P)H reduction of nitrate to nitrite. NR serves plants, algae, and fungi as a central point for integration of metabolism by governing flux of reduced nitrogen by several regulatory mechanisms. The NR monomer is composed of a similar to 100-kD polypeptide and one each of FAD, heme-iron, and molybdenum-molybdopterin (Mo-MPT). NR has eight sequence segments: (a) N-terminal "acidic" region; (b) Mo-MPT domain with nitrate-reducing active site; (c) interface domain; (d) Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; (e) cytochrome b domain; (f) Hinge 2; (g) FAD domain; and (h) NAD(P)H domain. The cytochrome b reductase fragment contains the active site where NAD(P)H transfers electrons to FAD. A complete three-dimensional dimeric NR structure model was built from structures of sulfite oxidase and cytochrome b reductase. Key active site residues have been investigated. NR structure, function, and regulation are now becoming understood.

引用

页码：277 / +

页数：28

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