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Nitrat reduktaza (hinon)
Identifikatori
EC broj	1.7.5.1
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Nitrat reduktaza (hinon) (EC 1.7.5.1, nitratna reduktaza A, nitratna reduktaza Z, hinol/nitratna oksidoreduktaza, hinol-nitratna oksidoreduktaza, hinol:nitrat oksidoreduktaza, NarA, NarZ, NarGHI) je enzim sa sistematskim imenom nitrit:hinon oksidoreduktaza.^[1]^[2]^[3]^[4]^[5]^[6]^[7] Ovaj enzim katalizuje sledeću hemijsku reakciju

nitrat + hinol

\rightleftharpoons

nitrit + hinon +H₂O

Ovaj za membranu vezani enzim učestvuje u anaerobnoj respiraciji.

Reference

↑ 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: 1234-1241. 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. 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: 5323-5329. 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: 14836-14843. PMID 15615728.
↑ Bonnefoy, V. and Demoss, J.A. (1994). „Nitrate reductases in Escherichia coli”. Antonie Van Leeuwenhoek 66: 47-56. 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: 61-68. 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: 679-687. PMID 2139607.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Nitrate+reductase+(quinone)

[1] 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: 1234-1241. PMID 4616697.

[2] 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. PMID 12910261.

[3] 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: 5323-5329. PMID 17439244.

[4] 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: 14836-14843. PMID 15615728.

[5] Bonnefoy, V. and Demoss, J.A. (1994). „Nitrate reductases in Escherichia coli”. Antonie Van Leeuwenhoek 66: 47-56. PMID 7747940.

[6] 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: 61-68. PMID 1321049.

[7] 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: 679-687. PMID 2139607.

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