Any feedback?
Information on EC 1.7.2.1 - nitrite reductase (NO-forming) and Organism(s) Paracoccus pantotrophus and UniProt Accession P72181
for references in articles please use BRENDA:EC1.7.2.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.7.2.1 nitrite reductase (NO-forming)IUBMB Comments
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.
Specify your search results
Word Map
- 1.7.2.1
- anemia
- mellitus
-
glycated
-
hematocrit
- erythrocyte
- hematological
- women
- arterial
-
glycemic
- transfusion
- platelet
- children
- albumin
- cardiovascular
- cholesterol
-
postoperative
- ferritin
- fetal
-
sickle
- creatinine
-
preoperative
- bleeding
- cardiac
- erythropoietin
- hypertension
- heme
- triglyceride
- hemorrhage
-
admission
-
systolic
- venous
-
demographic
-
january
-
hemolysis
-
c-reactive
-
erythroid
- hypoglycemia
-
comorbidities
- reticulocyte
-
hemodialysis
- transferrin
-
admitted
-
hemodynamic
-
placebo
-
diastolic
-
intraoperative
-
outpatient
-
anthropometric
- bilirubin
- waist
- medicine
- analysis
The taxonomic range for the selected organisms is: Paracoccus pantotrophus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hemoglobin, cunir, dissimilatory nitrite reductase, marc2, marc1, pseudomonas cytochrome oxidase, cytochrome cd1 nitrite reductase, cu-nir, axnir, cytochrome cd, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome c-551:O2, NO2- oxidoreductase
-
-
-
-
cytochrome cd
-
-
-
-
cytochrome oxidase
-
-
-
-
oxidase, Pseudomonas cytochrome
-
-
-
-
Pseudomonas cytochrome oxidase
-
-
-
-
reductase, nitrite (cytochrome)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nitric-oxide:ferricytochrome-c oxidoreductase
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.
CAS REGISTRY NUMBER
COMMENTARY
9027-00-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
anaerobic assay conditions
-
-
?
hydroxylamine + reduced pseudoazurin
NH3 + H2O + oxidized pseudoazurin
-
-
-
-
?
NH2OH + reduced cytochrome c550
NH3 + H2O + oxidized cytochrome c550
-
additional electron donor: horse heart cytochrome c
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
O2 + reduced pseudoazurin
H2O + oxidized pseudoazurin
-
-
-
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
additional information
?
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
-
?
additional information
?
-
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome cd1
cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine
-
cytochrome cd1
the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure
-
cytochrome cd1
the heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, binding structure, overview
-
heme
cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer
heme
heme c has bis-histidine ligation and FeIII heme d1 [d1(FeIII)] is bound by histidine and tyrosine. The cytochrome cd1 heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, structure, overview
heme
two hemes in cytochrome cd1, the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
in hemes c and d1, the cytochrome cd1 heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, FeIII heme d1 [d1(FeIII)] is bound by histidine and tyrosine, structure, overview
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NapC
-
c-type cytochrome with 4 bis-histidinyl coordinated hemes capable of reducing and hence activating oxidized cytochrome cd1 nitrite reductase
-
additional information
cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
additional information
-
cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
0.43
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
0.68
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
1.15
hydroxylamine
-
25°C, pH 7.0, electron donor horse heart cytochrome c
2.5
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.434
NH2OH
-
pre-reduced enzyme, electron donor horse heart cytochrome c
1.15
NH2OH
-
initially oxidized enzyme, electron donor horse heart cytochrome c
1.38
NH2OH
-
initially oxidized enzyme, electron donor cytochrome c550
0.007
nitrite
-
25°C, pH 7.0, electron donor horse heart cytochrome c
0.011
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
0.012
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
0.071
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.0073
NO2-
-
initially oxidized enzyme, electron donor horse heart cytochrome c
0.011
NO2-
-
pre-reduced enzyme, electron donor horse heart cytochrome c
0.067
NO2-
-
initially oxidized enzyme, electron donor cytochrome c550
0.15
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
0.16
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.166
O2
-
pre-reduced enzyme, electron donor horse heart cytochrome c
0.17
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
0.47
O2
-
initially oxidized enzyme, electron donor horse heart cytochrome c
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
hydroxylamine
-
25°C, pH 7.0, electron donor horse heart cytochrome c
3
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
3.2
hydroxylamine
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
3.5
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
6.4
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.08
NH2OH
-
initially oxidized enzyme, electron donor cytochrome c550
0.2
NH2OH
-
initially oxidized enzyme, electron donor horse heart cytochrome c
3
NH2OH
-
pre-reduced enzyme, electron donor horse heart cytochrome c
2.7
nitrite
-
25°C, pH 7.0, wild-type, without pre-reduction with dithionite
41
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
74
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
144
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
2.4
NO2-
-
initially oxidized enzyme, electron donor horse heart cytochrome c
41
NO2-
-
pre-reduced enzyme, electron donor horse heart cytochrome c
106
NO2-
-
all-ferric nitrite-bound complex, electron donor pseudoazurin
0.11
O2
-
initially oxidized enzyme, electron donor horse heart cytochrome c
2.8
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
3
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
6.4
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 5.4
5.4
5.7
5.8
6.2
6.3
5.1 - 5.4
-
hydroxylamine reduction, electron donor pseudoazurin, pre-reduced cytochrome cd1
5.4
-
hydroxylamine reduction, electron donor cytochrome c550, pre-reduced cytochrome cd1
5.7
-
nitrite reduction, electron donor cytochrome c550, pre-reduced cytochrome cd1
5.8
-
nitrite reduction, electron donor pseudoazurin, pre-reduced cytochrome cd1
6.2
-
O2 reduction, electron donor cytochrome c550, pre-reduced cytochrome cd1
6.3
-
O2 reduction, electron donor pseudoazurin, pre-reduced cytochrome cd1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NIRS_PARPN
596
0
65383
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of Y25S mutant protein are grown from a solution containing 10-20 mg/ml protein in the presence of 2.2-2.4 M ammonium sulfate and 50 mM potassium phosphate, pH 7.0, crystals diffract to 1.4 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M106H
-
inactive protein, the unusual highly cooperative and strongly hysteretic redox titration of the wild-type is lost in the mutant protein
Y25S
-
unlike the wild-type enzyme, the Y25S mutant is active as a reductase toward nitrite, O2, and hydroxylamine without a reduuctive activation step
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Silvestrini, M.C.; Falcinelli, S.; Ciabatti, I.; Cutruzzola, F.; Brunori, M.
Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview
Biochimie
76
641-654
1994
Alcaligenes faecalis, Paracoccus denitrificans, Halomonas halodenitrificans, Paracoccus pantotrophus, Pseudomonas aeruginosa, Pseudomonas stutzeri, Thiobacillus denitrificans
Ferguson, S.J.; Fulop, V.
Cytochrome cd1 nitrite reductase: structure raises interesting mechanistic questions
Subcell. Biochem.
35
519-540
2000
Paracoccus pantotrophus, Pseudomonas aeruginosa
Allen, J.W.; Higham, C.W.; Zajicek, R.S.; Watmough, N.J.; Ferguson, S.J.
A novel, kinetically stable, catalytically active, all-ferric, nitrite-bound complex of Paracoccus pantotrophus cytochrome cd1
Biochem. J.
366
883-888
2002
Paracoccus pantotrophus
Richter, C.D.; Allen, J.W.A.; Higham, C.W.; Koppenhofer, A.; Zajicek, R.S.; Watmough, N.J.; Ferguson, S.J.
Cytochrome cd1, reductive activation and kinetic analysis of a multifunctional respiratory enzyme
J. Biol. Chem.
277
3093-3100
2002
Paracoccus pantotrophus
Zajicek, R.S.; Allen, J.W.; Cartron, M.L.; Richardson, D.J.; Ferguson, S.J.
Paracoccus pantotrophus NapC can reductively activate cytochrome cd1 nitrite reductase
FEBS Lett.
565
48-52
2004
Paracoccus pantotrophus
Gordon, E.H.; Sjogren, T.; Lofqvist, M.; Richter, C.D.; Allen, J.W.; Higham, C.W.; Hajdu, J.; Fulop, V.; Ferguson, S.J.
Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine
J. Biol. Chem.
278
11773-11781
2003
Paracoccus pantotrophus
Zajicek, R.S.; Cartron, M.L.; Ferguson, S.J.
Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine
Biochemistry
45
11208-11216
2006
Paracoccus pantotrophus
Oganesyan, V.S.; Cheesman, M.R.; Thomson, A.J.
Magnetic circular dichroism evidence for a weakly coupled heme-radical pair at the active site of cytochrome cd1, a nitrite reductase
Inorg. Chem.
46
10950-10952
2007
Paracoccus pantotrophus (P72181)
van Wonderen, J.H.; Knight, C.; Oganesyan, V.S.; George, S.J.; Zumft, W.G.; Cheesman, M.R.
Activation of the cytochrome cd1 nitrite reductase from Paracoccus pantotrophus. Reaction of oxidized enzyme with substrate drives a ligand switch at heme c
J. Biol. Chem.
282
28207-28215
2007
Pseudomonas stutzeri (P24040), Pseudomonas stutzeri, Paracoccus pantotrophus (P72181), Paracoccus pantotrophus, Pseudomonas stutzeri ZoBell / ATCC 14405 (P24040)
EXTERNAL LINKS (specific for EC-Number 1.7.2.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
