| Entry |
|
|---|
| Name |
nitrite reductase (NO-forming);
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;
NO-forming) |
|---|
| Class |
Oxidoreductases;
Acting on other nitrogenous compounds as donors;
With a cytochrome as acceptor
 |
|---|
| Sysname |
nitric-oxide:ferricytochrome-c oxidoreductase |
|---|
| Reaction(IUBMB) |
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c
+ 2 H+ [RN:R00783] |
|---|
| Reaction(KEGG) |
R00783 > R00784;
(other) R00081 R00082 R00280 R00785
 |
|---|
| Substrate |
nitric oxide [CPD:C00533];
H2O [CPD:C00001];
ferricytochrome c [CPD:C00125] |
|---|
| Product |
nitrite [CPD:C00088];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080] |
|---|
| Cofactor |
FAD [CPD:C00016];
Iron [CPD:C00023];
Copper [CPD:C00070] |
|---|
| Comment |
The reaction is catalysed by two types of enzymes, found in the
perimplasm of denitrifying bacteria. One type comprises proteins
containing multiple copper centres, the other a heme protein,
cytochrome cd1. Acceptors include c-type cytochromes such as
cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans
or Pseudomonas aeruginosa, and small blue copper proteins such as
azurin and pseudoazurin. Cytochrome cd1 also has oxidase and
hydroxylamine reductase activities. May also catalyse the reaction
of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known
activity of cytochrome cd1. |
|---|
| Pathway |
PATH: ec00910 Nitrogen metabolism |
|---|
| Orthology |
KO: K00368 nitrite reductase (NO-forming) |
|---|
| Genes |
OSA: 4324803(Os01g0850800)
MSU: MS0876(sufI)
APL: APL_2035(sufI)
ASU: Asuc_0978
PAE: PA0519(nirS)
PAU: PA14_06750(nirS)
PFL: PFL_5501(nirK)
PEN: PSEEN5226
SDN: Sden_3482
SAZ: Sama_2681
SLO: Shew_3335
CPS: CPS_4220(nirS)
PHA: PSHAa1477
NOC: Noc_0089
HCH: HCH_04416
KKO: Kkor_2024
NMA: NMA1887
NME: NMB1623(pan1)
NMC: NMC1549(aniA)
NMI: NMO_1452(aniA)
NGO: NGO1276
CVI: CV_2007(aniA)
RSO: RS03038(RSp1503)
RPI: Rpic_4015
RPF: Rpic12D_4128
REU: Reut_B5010 Reut_B5018
REH: H16_B2277(nirS)
RME: Rmet_3172
BMA: BMAA0755 BMAA0798
BMV: BMASAVP1_0548 BMASAVP1_0593
BML: BMA10229_0659 BMA10229_0703
BMN: BMA10247_A1613 BMA10247_A1658
BPS: BPSS1452 BPSS1487
BPM: BURPS1710b_A0477(aniA) BURPS1710b_A0520
BPL: BURPS1106A_A1966 BURPS1106A_A2012(nirK)
BPD: BURPS668_A2061 BURPS668_A2107(nirK)
BTE: BTH_II0881 BTH_II0944
PNA: Pnap_1326
AJS: Ajs_1912
HAR: HEAR3245
NMU: Nmul_A1998
EBA: ebA888(nirS)
DAR: Daro_3323
TBD: Tbd_0077
MMB: Mmol_1061
APP: CAP2UW1_2489
TDN: Suden_1985
BBA: Bd2608
MES: Meso_2243 Meso_4273
PLA: Plav_1009
SME: SMa1250(nirK)
SMD: Smed_6278
ATU: Atu4382(nirK)
ATC: AGR_L_970
RET: RHE_PF00525(nirK)
RHI: NGR_c09950(nirK)
BME: BMEII0988
BMF: BAB2_0943
BMB: BruAb2_0919
BMS: BRA0260
BOV: BOV_A0236(nirK)
OAN: Oant_1108 Oant_4379
BJA: blr7089(nirK)
BRA: BRADO1227(nirK)
BBT: BBta_6826(nirK)
RPA: RPA3306(nirK1) RPA4145(nirK2)
RPE: RPE_4071
RPT: Rpal_4623
NWI: Nwi_2648
OCA: OCAR_7249
MSL: Msil_1519
SIL: SPOA0220(nirS)
RSQ: Rsph17025_1595
RDE: RD1_1565(nirS) RD1_1567(nirC) RD1_1568(nirF) RD1_1573(nirN)
PDE: Pden_2487
DSH: Dshi_3180(nirS)
MAG: amb4165
GKA: GK0767
GTN: GTNG_0650(nirK)
STH: STH741
LBI: LEPBI_I1063(aniA)
FJO: Fjoh_2418
CAU: Caur_1570
CAG: Cagg_1796
CHL: Chy400_1706
HYA: HY04AAS1_0339
NPH: NP1598A(nirK)
 |
|---|
| Structures |
PDB: 1GQ1 1RZP 1RZQ 1SJM 1SNR 1ZDQ 1ZDS 1ZV2 2A3T 2AVF
2B08 2BW4 2BW5 2BWD 2BWI 2DV6 2DWS 2DWT 2DY2 2E86
2FJS 2JFC 2P80 2PP7 2PP8 2PP9 2PPA 2PPC 2PPD 2PPE
2PPF 2VW4 2VW6 2VW7 2ZON 2ZOO |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:5354021]
Miyata M, Mori T.
Studies on denitrification. X. The "denitrifying enzyme"
as a nitrite reductase and the electron donating system for
denitrification.
J. Biochem. (Tokyo). 66 (1969) 463-71.
Pseudomonas denitrificans |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:13295215]
CHUNG CW, NAJJAR VA.
Cofactor requirements for enzymatic denitrification. I. Nitrite
reductase.
J. Biol. Chem. 218 (1956) 617-25.
Pseudomonas stutzeri [GN:psa] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:13782716]
WALKER GC, NICHOLAS DJ.
Nitrite reductase from Pseudomonas aeruginosa.
Biochim. Biophys. Acta. 49 (1961) 350-60.
Pseudomonas aeruginosa |
|---|
Reference
Authors
Title
Journal
|
4
Singh, J.
Cytochrome oxidase from Pseudomonas aeruginosa. III. Reduction of
hydroxylamine.
Biochim. Biophys. Acta 333 (1974) 28-36. |
|---|
Reference
Authors
Title
Journal
|
5
Michalski, W.P. and Nicholas, D.J.D.
Molecular characterization of a copper-containing nitrite reductase
from Rhodopseudomonas sphaeriodes forma sp. Denitrificans.
Biochim. Biophys. Acta 828 (1985) 130-137. |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:1862344]
Godden JW, Turley S, Teller DC, Adman ET, Liu MY, Payne WJ, LeGall
J.
The 2.3 angstrom X-ray structure of nitrite reductase from
Achromobacter cycloclastes.
Science. 253 (1991) 438-42.
Achromobacter cycloclastes |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:7583671]
Williams PA, Fulop V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson
SJ, Radford SE, Hajdu J.
Pseudospecific docking surfaces on electron transfer proteins as
illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1
nitrite reductase.
Nat. Struct. Biol. 2 (1995) 975-82.
Thiosphaera pantotropha |
|---|
Reference
Authors
Title
Journal
Organism
|
8 [PMID:8639023]
Hole UH, Vollack KU, Zumft WG, Eisenmann E, Siddiqui RA, Friedrich
B, Kroneck PM.
Characterization of the membranous denitrification enzymes nitrite
reductase (cytochrome cd1) and copper-containing nitrous oxide
reductase from Thiobacillus denitrificans.
Arch. Microbiol. 165 (1996) 55-61.
Thiobacillus denitrificans [GN:tbd] |
|---|
Reference
Authors
Title
Journal
Organism
|
9 [PMID:9409151]
Zumft WG.
Cell biology and molecular basis of denitrification.
Microbiol. Mol. Biol. Rev. 61 (1997) 533-616.
Thiobacillus denitrificans [GN:tbd], Roseobacter denitrificans
[GN:rde], Paracoccus denitrificans [GN:pde], Alcaligenes faecalis,
Azospirillum brasilense, Halomonas halodenitrificans,
Magnetospirillum magnetotacticum, Pseudomonas aeruginosa,
Pseudomonas nautica, Pseudomonas stutzeri [GN:psa], Ralstonia
eutropha |
|---|
Reference
Authors
Title
Journal
Organism
|
10 [PMID:9667932]
Ferguson SJ.
Nitrogen cycle enzymology.
Curr. Opin. Chem. Biol. 2 (1998) 182-93.
Pseudomonas aeruginosa |
|---|
Reference
Authors
Title
Journal
Organism
|
11 [PMID:9308169]
Vijgenboom E, Busch JE, Canters GW.
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 ( Pt 9) (1997) 2853-63.
Pseudomonas aeruginosa [GN:pae] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.7.2.1
IUBMB Enzyme Nomenclature: 1.7.2.1
ExPASy - ENZYME nomenclature database: 1.7.2.1
BRENDA, the Enzyme Database: 1.7.2.1
CAS: 9080-03-9 |
|---|
