Any feedback?
Information on EC 1.7.2.1 - nitrite reductase (NO-forming) and Organism(s) Pseudomonas stutzeri and UniProt Accession P24040
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: Pseudomonas stutzeri
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 + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
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, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
?
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, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
?
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 + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
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. Spectral analysis, overview
-
heme
heme c and heme d1, cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
Calmels, S.; Ohshima, H.; Henry, Y.; Bartsch, H.
Characterization of bacterial cytochrome cd(1)-nitrite reductase as one enzyme responsible for catalysis of nitrosation of secondary amines
Carcinogenesis
17
533-536
1996
Pseudomonas aeruginosa, Pseudomonas stutzeri
Hartig, E.; Zumft, W.G.
Kinetics of nirS expression (cytochrome cd1 nitrite reductase) in Pseudomonas stutzeri during the transition from aerobic respiration to denitrification: evidence for a denitrification-specific nitrate- and nitrite-responsive regulatory system
J. Bacteriol.
181
161-166
1999
Pseudomonas stutzeri
Farver, O.; Kroneck, P.M.; Zumft, W.G.; Pecht, I.
Intramolecular electron transfer in cytochrome cd(1) nitrite reductase from Pseudomonas stutzeri; kinetics and thermodynamics
Biophys. Chem.
98
27-34
2002
Pseudomonas stutzeri
Farver, O.; Kroneck, P.M.; Zumft, W.G.; Pecht, I.
Allosteric control of internal electron transfer in cytochrome cd1 nitrite reductase
Proc. Natl. Acad. Sci. USA
100
7622-7625
2003
Pseudomonas stutzeri, Pseudomonas stutzeri ZoBell / ATCC 14405
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
