KEGG   ENZYME: 1.7.2.1Help
Entry
EC 1.7.2.1                  Enzyme                                 

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
BRITE hierarchy
Sysname
nitric-oxide:ferricytochrome-c oxidoreductase
Reaction(IUBMB)
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ [RN:R00783]
Reaction(KEGG)
Substrate
nitric oxide [CPD:C00533];
H2O [CPD:C00001];
ferricytochrome c [CPD:C00125]
Product
nitrite [CPD:C00088];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
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.
History
EC 1.7.2.1 created 1961, modified 1976, modified 2001, modified 2002 (EC 1.7.99.3 created 1961 as EC 1.6.6.5, transferred 1964 to EC 1.7.99.3, modified 1976, incorporated 2002, EC 1.9.3.2 created 1965, incorporated 2002)
Pathway
Nitrogen metabolism
Microbial metabolism in diverse environments
Orthology
K00368  
nitrite reductase (NO-forming)
K15864  
nitrite reductase (NO-forming) / hydroxylamine reductase
Genes
HPR: 
MSU: 
MS0876(sufI)
APL: 
APL_2035(sufI)
APJ: 
APJL_2086(sufI2)
APA: 
ASU: 
ASI: 
ASS: 
GAN: 
PSU: 
RHD: 
DJI: 
DJA: 
PAE: 
PA0519(nirS)
PAEV: 
N297_531(nirS)
PAEI: 
N296_531(nirS)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAER: 
PAEM: 
PAEL: 
PAES: 
PAEU: 
PAEG: 
PAEC: 
M802_530(nirS)
PAEO: 
M801_531(nirS)
PMOS: 
PFL: 
PFL_5501(nirK)
PPRC: 
PFE: 
PEN: 
PMK: 
PSA: 
PST_3532(nirS)
PSZ: 
PSR: 
PSC: 
PSJ: 
PSH: 
PSTU: 
PSTT: 
PBA: 
PBC: 
PDR: 
PSK: 
PCH: 
PCP: 
MCT: 
MCR_0135(aniA)
MCS: 
DR90_1762(nirK)
MCAT: 
SDN: 
SAZ: 
SLO: 
SWD: 
ILO: 
ILI: 
CPS: 
CPS_4220(nirS)
PHA: 
MAQ: 
MHC: 
MARHY3064(nirS)
MBS: 
MEC: 
NOC: 
NHL: 
TKM: 
TNI: 
HCH: 
ADI: 
KKO: 
OCE: 
GPB: 
NMA: 
NME: 
NMB1623(pan1)
NMP: 
NMH: 
NMC: 
NMC1549(aniA)
NMI: 
NMO_1452(aniA)
NMM: 
NMS: 
NMW: 
NMAA_1353(aniA)
NMZ: 
NGO: 
NGK: 
NGT: 
NLA: 
NLA_6490(aniA)
CVI: 
CV_2007(aniA)
PSE: 
NH8B_1422(nirS)
RSO: 
RS03038(RSp1503)
RSL: 
RSN: 
RSM: 
RSE: 
RPI: 
RPF: 
RPJ: 
REU: 
REH: 
H16_B2277(nirS)
CNC: 
RME: 
Rmet_3172(nirS)
CTI: 
BMA: 
BMV: 
BML: 
BMN: 
BMAL: 
BPS: 
BPM: 
BPL: 
BPD: 
BPSE: 
BPSM: 
BPSU: 
BPSD: 
BPZ: 
BPQ: 
BPK: 
BPSH: 
BTE: 
BTQ: 
BTJ: 
BTZ: 
BTD: 
BTI_3972(nirK)
BTV: 
BTHE: 
BTHM: 
BOK: 
DM82_5662(nirK)
BUT: 
BPT: 
Bpet4054(nirS)
AXY: 
AXO: 
AXN: 
AXS: 
TEQ: 
TEA: 
KUI_1530(nirK2)
TEG: 
KUK_0832(nirK2)
TAS: 
TAT: 
KUM_0196(nirK2)
PUT: 
CDN: 
BPSI: 
PNA: 
AJS: 
DIA: 
ADN: 
ADK: 
HAR: 
LCH: 
RGE: 
RGE_06580(nirS)
NEU: 
NE0924(aniA)
NET: 
NIT: 
NII: 
NMU: 
EBA: 
ebA888(nirS)
AZA: 
AZKH_3548(nirS) AZKH_p0630(nirK_aniA)
DAR: 
TMZ: 
DSU: 
TBD: 
SDR: 
MMB: 
APP: 
SLT: 
NIS: 
BBA: 
BBAT: 
BBW: 
BBAC: 
MCI: 
MOP: 
MAM: 
MES: 
PLA: 
SME: 
SMa1250(nirK)
SMQ: 
SMI: 
SMEG: 
SMEL: 
SMER: 
SMD: 
RHI: 
SFH: 
SFD: 
EAD: 
ATU: 
Atu4382(nirK)
RET: 
REL: 
RIR: 
NGL: 
NGG: 
BME: 
BMI: 
BMZ: 
BMG: 
BMW: 
BMEE: 
DK62_3139(nirK)
BMF: 
BMB: 
BMC: 
BAA: 
BABO: 
DK55_2887(nirK)
BABR: 
DO74_2202(nirK)
BMS: 
BSI: 
BSF: 
BSUI: 
BMT: 
BSZ: 
DK67_2279(nirK)
BSV: 
BSW: 
BSG: 
BOV: 
BOV_A0236(nirK)
BCS: 
BSK: 
BOL: 
BCAR: 
DK60_3132(nirK)
BCAS: 
BMR: 
BMI_II254(nirK)
BPP: 
BPI_II255(nirK)
BPV: 
DK65_2218(nirK)
BCET: 
BCEE: 
OAN: 
OAH: 
DR92_3865(nirK) DR92_659(nirK)
BJA: 
blr7089(nirK)
BJU: 
BRA: 
BRADO1227(nirK)
BBT: 
BBta_6826(nirK)
BRS: 
S23_12320(nirK)
AOL: 
RPA: 
RPA3306(nirK1) RPA4145(nirK2)
RPE: 
RPT: 
RPX: 
NWI: 
NHA: 
OCA: 
OCG: 
OCA5_c08660(aniA1) OCA5_c25200(aniA2)
OCO: 
OCA4_c08650(aniA1) OCA4_c25190(aniA2)
SNO: 
MSL: 
HDN: 
HDT: 
HNI: 
CSE: 
PZU: 
SIL: 
SPOA0220(nirS)
RSQ: 
RSK: 
RDE: 
RD1_1565(nirS) RD1_1567(nirC) RD1_1568(nirF)
RLI: 
PDE: 
DSH: 
Dshi_3180(nirS)
PSF: 
PSE_0898(nirS)
PGA: 
PGL: 
PGD: 
OAT: 
LMD: 
SWI: 
MAG: 
MGY: 
AZL: 
ALI: 
ABS: 
PGV: 
GKA: 
GTN: 
GTNG_0650(nirK)
GTH: 
GCT: 
GMC: 
GJF: 
GST: 
VIR: 
STH: 
TMR: 
SAY: 
SAP: 
MIR: 
MID: 
MVA: 
MGI: 
MSP: 
MJD: 
CEF: 
CDI: 
CDP: 
CDH: 
CDT: 
CDE: 
CDA: 
CDZ: 
CDS: 
CDD: 
CDW: 
CDV: 
CUR: 
CUA: 
CAR: 
CKP: 
CPU: 
CPL: 
CPG: 
CPP: 
CPK: 
CPQ: 
CPX: 
CPZ: 
COR: 
COD: 
COS: 
COI: 
COE: 
COU: 
CHN: 
CCN: 
CMD: 
CVT: 
CAX: 
COA: 
AAI: 
RMU: 
RDN: 
BFA: 
JDE: 
XCE: 
CFL: 
CFI: 
CGA: 
ICA: 
PAC: 
PAK: 
PAV: 
PAX: 
PAZ: 
PAW: 
PAD: 
PCN: 
PACC: 
PACH: 
PFR: 
PPC: 
PBO: 
PRA: 
MPH: 
NCA: 
TFU: 
SRO: 
ACE: 
BSD: 
TBI: 
AMI: 
MAU: 
MIL: 
AMS: 
BAST: 
BCOR: 
OTE: 
MIN: 
Minf_0929(sufI)
LBI: 
LBF: 
TPX: 
GAU: 
GAU_2766(nirK)
GBA: 
RMR: 
RMG: 
SCN: 
BBD: 
MTT: 
FJO: 
FCO: 
FBC: 
MRS: 
ASL: 
FBA: 
RCA: 
CAU: 
CAG: 
CHL: 
HAU: 
STI: 
ATM: 
ANT_27710(nirS)
TTS: 
TTL: 
TSC: 
TOS: 
OPR: 
HYA: 
HTH: 
HTH_0150(nirS)
HTE: 
SUL: 
PMX: 
NDE: 
LFP: 
TTR: 
MOX: 
DAMO_2415(nirS)
HMA: 
rrnAC2853(nirK)
HHI: 
HAH_0129(nirK)
HHN: 
NPH: 
NP1598A(nirK)
HUT: 
HMU: 
HTU: 
HVO: 
HVO_2141(nirK)
HME: 
HFX_2183(aniA)
HBO: 
HXA: 
NAT: 
NPE: 
HRU: 
SALI: 
ACJ: 
NMR: 
NIR: 
NKR: 
NGA: 
NVN: 
NEV: 
CSU: 
 » show all
Taxonomy
Reference
1  [PMID:5354021]
  Authors
Miyata M, Mori T.
  Title
Studies on denitrification. X. The "denitrifying enzyme" as a nitrite reductase and the electron donating system for denitrification.
  Journal
J. Biochem. (Tokyo). 66 (1969) 463-71.
Reference
2  [PMID:13295215]
  Authors
CHUNG CW, NAJJAR VA.
  Title
Cofactor requirements for enzymatic denitrification.  I.  Nitrite reductase.
  Journal
J. Biol. Chem. 218 (1956) 617-25.
Reference
3  [PMID:13782716]
  Authors
WALKER GC, NICHOLAS DJ.
  Title
Nitrite reductase from Pseudomonas aeruginosa.
  Journal
Biochim. Biophys. Acta. 49 (1961) 350-60.
Reference
4
  Authors
Singh, J.
  Title
Cytochrome oxidase from Pseudomonas aeruginosa. III. Reduction of hydroxylamine.
  Journal
Biochim. Biophys. Acta 333 (1974) 28-36.
Reference
5
  Authors
Michalski, W.P. and Nicholas, D.J.D.
  Title
Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaeriodes forma sp. Denitrificans.
  Journal
Biochim. Biophys. Acta 828 (1985) 130-137.
Reference
6  [PMID:1862344]
  Authors
Godden JW, Turley S, Teller DC, Adman ET, Liu MY, Payne WJ, LeGall J.
  Title
The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes.
  Journal
Science. 253 (1991) 438-42.
  Sequence
[up:P25006]
Reference
7  [PMID:7583671]
  Authors
Williams PA, Fulop V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson SJ, Radford SE, Hajdu J.
  Title
Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase.
  Journal
Nat. Struct. Biol. 2 (1995) 975-82.
Reference
8  [PMID:8639023]
  Authors
Hole UH, Vollack KU, Zumft WG, Eisenmann E, Siddiqui RA, Friedrich B, Kroneck PM.
  Title
Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans.
  Journal
Arch. Microbiol. 165 (1996) 55-61.
  Sequence
[tbd:Tbd_0077]
Reference
9  [PMID:9409151]
  Authors
Zumft WG.
  Title
Cell biology and molecular basis of denitrification.
  Journal
Microbiol. Mol. Biol. Rev. 61 (1997) 533-616.
Reference
10 [PMID:9667932]
  Authors
Ferguson SJ.
  Title
Nitrogen cycle enzymology.
  Journal
Curr. Opin. Chem. Biol. 2 (1998) 182-93.
Reference
11 [PMID:9308169]
  Authors
Vijgenboom E, Busch JE, Canters GW.
  Title
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.
  Journal
Microbiology. 143 ( Pt 9) (1997) 2853-63.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9080-03-9

DBGET integrated database retrieval system