Nitrite reductase (NO-forming)
| nitrite reductase (NO-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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Nitrite reductase trimer, Alcaligenes faecalis | |||||||||
| Identifiers | |||||||||
| EC number | 1.7.2.1 | ||||||||
| CAS number | 37256-41-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a nitrite reductase (NO-forming) (EC 1.7.2.1) is an enzyme that catalyzes the chemical reaction
- nitric oxide + H2O + ferricytochrome c ⇌ nitrite + ferrocytochrome c + 2 H+
The 3 substrates of this enzyme are nitric oxide, H2O, and ferricytochrome c, whereas its 3 products are nitrite, ferrocytochrome c, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is nitric-oxide:ferricytochrome-c oxidoreductase. Other names in common use include cd-cytochrome nitrite reductase, [nitrite reductase (cytochrome)] [misleading, see comments.], cytochrome c-551:O2, NO2+ oxidoreductase, cytochrome cd, cytochrome cd1, hydroxylamine (acceptor) reductase, methyl viologen-nitrite reductase, nitrite reductase (cytochrome, and NO-forming). This enzyme participates in nitrogen metabolism. It has 3 cofactors: FAD, Iron, and Copper.
Structural studies
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1RZP, 1RZQ, 1SJM, 1SNR, 1ZDQ, 1ZDS, 1ZV2, 2A3T, 2AVF, 2B08, 2BW4, 2BW5, 2BWD, 2BWI, 2DV6, 2DWS, 2DWT, 2DY2, 2FJS, and 2JFC.
References
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- Walker GC, Nicholas DJ (1961). "Nitrite reductase from Pseudomonas aeruginosa". Biochim. Biophys. Acta. 49 (2): 350–360. PMID 13782716. doi:10.1016/0006-3002(61)90134-2.
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- Michalski WP, Nicholas DJ (1985). "Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaeriodes forma sp. Denitrificans". Biochim. Biophys. Acta. 828 (2): 130–137. doi:10.1016/0167-4838(85)90048-2.
- Godden JW; Turley, S; Teller, DC; Adman, ET; Liu, MY; Payne, WJ; Legall, J (1991). "The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes". Science. 253 (5018): 438–442. PMID 1862344. doi:10.1126/science.1862344.
- Williams PA, Fülöp V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson SJ, Radford SE, Hajdu J (1995). "Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase". Nat. Struct. Biol. 2 (11): 975–982. PMID 7583671. doi:10.1038/nsb1195-975.
- B, Kroneck PM; Vollack, KU; Zumft, WG; Eisenmann, E; Siddiqui, RA; Friedrich, B; Kroneck, PM (1996). "Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans". Arch. Microbiol. 165 (1): 55–61. PMID 8639023. doi:10.1007/s002030050296.
- Zumft WG (1997). "Cell biology and molecular basis of denitrification". Microbiol. Mol. Biol. Rev. 61 (4): 533–616. PMC 232623
. PMID 9409151. - Ferguson SJ (1998). "Nitrogen cycle enzymology". Curr. Opin. Chem. Biol. 2 (2): 182–193. PMID 9667932. doi:10.1016/S1367-5931(98)80059-8.
- Vijgenboom E, Busch JE, Canters GW (September 1997). "In vivo studies disprove an obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under control of rpoS and ANR". Microbiology. 143 (9): 2853–2863. PMID 9308169. doi:10.1099/00221287-143-9-2853.