Nitrate reductase (quinone)

Nitrate reductase (quinone) (EC 1.7.5.1, nitrate reductase A, nitrate reductase Z, quinol/nitrate oxidoreductase, quinol-nitrate oxidoreductase, quinol:nitrate oxidoreductase, NarA, NarZ, NarGHI) is an enzyme with systematic name nitrite:quinone oxidoreductase.^[1]^[2]^[3]^[4]^[5]^[6]^[7] This enzyme catalyses the following chemical reaction

nitrate + a quinol

\rightleftharpoons

nitrite + a quinone + H₂O

This is a membrane-bound enzyme which supports [anaerobic respiration] on nitrate.

References

↑ Enoch, H.G. and Lester, R.L. (1974). "The role of a novel cytochrome b-containing nitrate reductase and quinone in the in vitro reconstruction of formate-nitrate reductase activity of E. coli". Biochem. Biophys. Res. Commun. 61 (4): 1234–1241. doi:10.1016/s0006-291x(74)80416-x. PMID 4616697.
↑ Bertero, M.G., Rothery, R.A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J.H. and Strynadka, N.C. (2003). "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A". Nat. Struct. Biol. 10: 681–687. doi:10.1038/nsb969. PMID 12910261.
↑ Lanciano, P., Magalon, A., Bertrand, P., Guigliarelli, B. and Grimaldi, S. (2007). "High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme b_D". Biochemistry 46 (18): 5323–5329. doi:10.1021/bi700074y. PMID 17439244.
↑ Bertero, M.G., Rothery, R.A., Boroumand, N., Palak, M., Blasco, F., Ginet, N., Weiner, J.H. and Strynadka, N.C. (2005). "Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A". J. Biol. Chem. 280 (15): 14836–14843. doi:10.1074/jbc.M410457200. PMID 15615728.
↑ Bonnefoy, V. and Demoss, J.A. (1994). "Nitrate reductases in Escherichia coli". Antonie Van Leeuwenhoek 66 (1-3): 47–56. doi:10.1007/bf00871632. PMID 7747940.
↑ Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G. and Bertrand, P. (1992). "EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism". Eur. J. Biochem. 207 (1): 61–68. doi:10.1111/j.1432-1033.1992.tb17020.x. PMID 1321049.
↑ Iobbi-Nivol, C., Santini, C.L., Blasco, F. and Giordano, G. (1990). "Purification and further characterization of the second nitrate reductase of Escherichia coli K12". Eur. J. Biochem. 188 (3): 679–687. doi:10.1111/j.1432-1033.1990.tb15450.x. PMID 2139607.

External links

Nitrate reductase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: nitrogenous donor (EC 1.7)

1.7.1	GMP reductase

1.7.2	Nitrite reductase (NO-forming)

1.7.3	Urate oxidase

1.7.7	Ferredoxin—nitrite reductase

1.7.99	Hydroxylamine reductase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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