1932

Abstract

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 ∼100-kD polypeptide and one each of FAD, heme-iron, and molybdenum-molybdopterin (Mo-MPT). NR has eight sequence segments: () -terminal “acidic” region; () Mo-MPT domain with nitrate-reducing active site; () interface domain; () Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; () cytochrome b domain; () Hinge 2; () FAD domain; and () 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.

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/content/journals/10.1146/annurev.arplant.50.1.277
1999-06-01
2024-06-16
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  • Article Type: Review Article
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