The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology
Abstract
▪ 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: (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.
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Citations
Cites
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596
Karplus, P. A., Daniels, M. J., & Herriott, J. R. (1991) · Science · doi:10.1126/science.1986412 · Cited by 536
Cited by
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872
Trace metal metabolism in plants
Andresen, E., Peiter, E., & Küpper, H. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/erx465 · Cited by 431
Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Metadata
- Authors
- Campbell, W. H.
- Venue
- Annual Review of Plant Physiology and Plant Molecular Biology
- Publisher
- Annual Reviews
- Published
- 1999-06
- Volume
- 50
- Issue
- 1
- Pages
- 277-303
- ISSN
- 1040-2519 (ISSN-L)
- OpenAlex
- W2097653436
- Cited by
- 772
- References
- 4
- FWCI
- 32.23
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology. https://app.cochat.ai/papers/10.1146/annurev.arplant.50.1.277
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- Campbell, W. H. (1999). NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology. Annual Review of Plant Physiology and Plant Molecular Biology. https://doi.org/10.1146/annurev.arplant.50.1.277
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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