HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.7.2.1 - nitrite reductase (NO-forming)
for references in articles please use BRENDA:EC1.7.2.1
Word Map on EC 1.7.2.1
- 1.7.2.1
- diabetes
- anemia
- erythrocyte
- mellitus
-
hematocrit
- women
- arterial
- transfusion
- renal
- hematological
- children
- platelet
-
glycated
- cholesterol
-
glycemic
-
sickle
- cardiovascular
- heme
- bone
-
postoperative
- marrow
- bleeding
- cardiac
- creatinine
- ferritin
- triglyceride
-
erythropoietin
-
enrol
-
preoperative
-
systolic
-
cross-sectional
-
hemodialysis
-
hemolysis
- venous
- hypertension
- hemorrhage
-
hemodynamic
-
c-reactive
-
demographic
-
transferrin
-
diastolic
-
admission
-
placebo
- bilirubin
-
erythroid
- reticulocyte
-
myoglobin
-
outpatient
-
intraoperative
- analysis
- medicine
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.7.2.1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
nitrite reductase (NO-forming)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
proposed reaction mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron-transfer mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron transfer from c heme to d1 heme is very slow, order of seconds
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
rate constants of intermolecular electron transfer
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
a copper protein, cytochrome c-552 or cytochrome c-553 from Pseudomonas denitrificans acts as acceptor
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
ordered mechanism in which electron transfer is gated by binding of nitrite to the type 2 Cu centre
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. The transformation from the initial O-coordination of substrate to the final N-coordination of product is achieved by electron transfer from T1 copper to T2 copper, rather than by the previously reported side-on coordination of a NO intermediate, which only takes place in the reduced enzyme. Role of structural change in the critical residue Asp98, which affects the energetics of substrate attachment and product release at the T2 copper reaction center, while it does not significantly affect the activation energy and reaction pathways of the nitrite reduction process
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
the proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, proton-coupled electron transfer is one of the key processes in enzyme reactions, density functional theory calculations analysis. The reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite. Reaction mechanism, overview
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction; the proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, proton-coupled electron transfer is one of the key processes in enzyme reactions, density functional theory calculations analysis. The reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite. Reaction mechanism, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9027-00-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pseudomonas stutzeri ZoBell / ATCC 14405
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
strain 2.4.3
-
-
-
-
-
-
395063, 395064, 395065, 395067, 395068, 395070, 395073, 395078, 660418, 663639, 663750, 663917, 663921, 664919, 664927, 665353, 665432, 665433, 666008, 666948, 673563, 698274, 724606, 741819
-
-
addition of nitrate to oxygen-limited cells induces cytochrome cd1 synthesis
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
metabolism
-
the enzyme is involved in the denitrification anoxic process, which occurs in four reduction steps: initial conversion of nitrate to nitrite, followed by transformation of nitrite to nitric oxide, subsequent reduction of nitric oxide to nitrous oxide, and the final conversion of nitrous oxide to dinitrogen gas. All stages are catalyzed by complex metalloenzymes with different transition metal cofactors. Dissimilatory nitrite reductases (NiRs) catalyze the reduction of nitrite to nitric oxide, the committed step in denitrification. There are two main types: one containing iron (cd1NiRs) and the other copper (CuNiRs)
metabolism
-
the enzyme catalyzes the key reaction in denitrification as the nitrogen compound is changed from an ionic state to a gaseous molecule
metabolism
-
the enzyme catalyzes the key reaction in denitrification as the nitrogen compound is changed from an ionic state to a gaseous molecule
-
physiological function
deletion of cytochrome cd1-type nitrite reductase NirS gene or gene NirN results in impaired growth and smaller, fewer, and aberrantly shaped magnetite crystals during nitrate reduction. Nitrite reduction is completely abolished in the DELTAnirS mutant. NirN is required for full reductase activity of NirS by maintaining a proper form of d1 heme for holo-cytochrome cd1 assembly
physiological function
-
dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
-
copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO2 ) to nitric oxide (NO) during denitrification
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO2 ) to nitric oxide (NO) during denitrification; dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
additional information
-
determination of the activation energies, transition states, and minimum energy pathways of CuNiR for reaction mechanism analysis. Structure modelling of the CuNiR active site involving residues His100, His135, His306, Asp98, His255, Ile257 and four water molecules. Structure-function analysis, detailed overview
additional information
-
geometric structure of the nitrite-bound T2 Cu site in GtNiR using density functional theory, DFT, calculations. The reduction of T2 Cu site promotes the proton transfer. Optimized structures of nitrite binding forms under physiological pH conditions and in neutral states, detailed overview
additional information
-
geometric structure of the nitrite-bound T2 Cu site in GtNiR using density functional theory, DFT, calculations. The reduction of T2 Cu site promotes the proton transfer. Optimized structures of nitrite binding forms under physiological pH conditions and in neutral states, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
hydroxylamine + reduced pseudoazurin
NH3 + H2O + oxidized pseudoazurin
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + oxidized benzyl viologen
?
-
-
-
-
?
NH2OH + reduced cytochrome c550
NH3 + H2O + oxidized cytochrome c550
-
additional electron donor: horse heart cytochrome c
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
-
-
-
-
?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + 2 H+
-
-
-
?
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
-
-
-
-
?
nitric oxide + H2O + oxidized phenazine methosulfate
nitrite + reduced phenazine methosulfate + 2 H+
-
phenazine methosulfate can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
-
-
?
nitric oxide + H2O + oxidized phenosafranin
nitrite + reduced phenosafranin + 2 H+
-
phenosafranin can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
-
-
?
nitrite + dithionite
NO + reduced dithionite
-
type 1 copper of the fully loaded protein is reduced both directly by dithionite and indirectly by the type 2 copper site via intramolecular electron transfer
-
-
?
nitrite + ferrocytochrome b5 + 2 H+
nitric oxide + H2O + ferricytochrome b5
-
-
-
?
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
-
anaerobic assay conditions
-
-
?
nitrite + methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced azurin
NO + oxidized azurin
-
azurin purified from Pseudomonas chlororaphis
-
-
?
nitrite + reduced benzyl viologen
nitric oxide + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen
-
random sequential mechanism
-
-
?
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
NO2 + reduced methyl viologen
NO + oxidized methylviologen
-
-
-
?
NO2- + morpholine
N-nitrosomorpholine
-
in the presence of diethyldithiocarbamic acid ethylester, nitrosation through the production of NO or NO+-like species
-
?
NO2- + Na2S2O4
NO + Na2S2O3
-
pysiological electron donor is unknown, no activity with methyl viologen, phenazine methosulfate or N,N,N',N',-tetramethyl-p-phenylenediamine
-
?
NO2- + reduced azurin
NO + oxidized azurin
-
putative physiological electron donor
-
?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
O2 + reduced pseudoazurin
H2O + oxidized pseudoazurin
-
-
-
-
?
O2-. + H+
H2O2 + O2
-
purified enzyme shows superoxide dismutase activity, approx. one-third that of pure superoxide dismutase
-
-
reduced tetramethyl-4-phenylenediamine + NO2
oxidized tetrametyl-4-phenylenediamine + NO
-
no reaction with horse ferrocytochrome c, Neurospora europaea ferrocytochrome c-552, Magnetospirillum magnetotacticum ferrocytochrome c-550 and Pseudomonas aeruginosa cytochrome c-551
-
?
reduced tetramethyl-4-phenylenediamine + O2
oxidized tetrametyl-4-phenylenediamine + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
in the presence of ascorbate, N,N,N',N-tetramethyl-p-phenylenediamine and cytochrome c-553
-
?
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
also reacts with horse heart cytochrome c
-
-
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
inactive with eukaryotic cytochromes c
-
-
nitrite + electron donor
NO + oxidized electron donor + H2O
-
mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donors: reduced methyl viologen, phenazine methosulfate and to a lesser extend hydroquinone, highly purified enzyme has cytochrome c oxidase activity
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donor: reduced benzyl viologen
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donors: thionine, brilliant cresyl blue, methylene blue, 2,6-dichlorophenolindophenol or Pseudomonas stutzeri cytochrome c-552 and 558
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donor: reduced benzyl viologen
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
Pseudomonas stutzeri ZoBell / ATCC 14405
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
-
-
-
-
?
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
-
-
-
?
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
-
reduction of pseudoazurin by ascorbate
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
-
reduction of pseudoazurin by ascorbate
-
-
?
nitrite + reduced azurin
NO + H2O + oxidized azurin
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
random sequential mechanism
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
-
-
-
?
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
pseudoazurin from Achromobacter cycloclastes
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
random sequential mechanism
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
cytochrome c550 and pseudoazurin are the alternative electron mediator proteins between the cytochrome bc1 and the cytochrome cd1 type nitrite reductase
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
role in respiration
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
-
NO2- + reduced ascorbate
NO + oxidized ascorbate
-
physiological electron donor is not known, 7% activity if NADH is used as artificial electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
reduced azurin + O2
oxidized azurin + H2O
-
putative physiological electron donor
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
-
additional information
?
-
-
theoretical investigation has provided a number of insights into the reaction mechanism of copper nitrite reductase: The results presented in this paper indicate that the hydroxyl-intermediate pathway appears unlikely for the main reaction. The results also indicate that Asp-92 may play a significant structural role through hydrogen-bonding to the protonated oxygen of the nitrite substrate, and thereby elongating the N O bond, which is to be cleaved
-
-
-
additional information
?
-
density functional theory study of nitrite and nitric oxide adducts
-
-
-
additional information
?
-
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
-
additional information
?
-
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
-
additional information
?
-
-
cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
-
-
-
additional information
?
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
-
additional information
?
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
-
additional information
?
-
a conserved and functional aniA gene is not essential for meningococcal survival
-
-
-
additional information
?
-
-
simulation of the NO kinetics observed in batch cultures of Paracoccus denitrificans, including aerobic and anaerobic growth, the kinetics of O2 consumption and denitrification. The model predicts NO concentrations close to that measured. The predicted steady-state NO aqueous concentration for an actively denitrifying population is 35 nM
-
-
-
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
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
additional information
?
-
-
nitrite reductase in both oxidized and reduced states forms with NO two distinct compounds at both hemes. These compounds, in addition to the oxidized and reduced enzymes, are formed during the turnover of this enzyme as functional intermediates
-
-
-
additional information
?
-
-
spectroscopic analysis of the reactivity of cd1NiR and its semi-apo derivative with NO. The c heme nitrosylation is enhanced during catalysis
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
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
?
-
Pseudomonas stutzeri ZoBell / ATCC 14405
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
?
-
-
electrocatalytic reduction of nitrite to NO by CuMe2bpaCl2, as a model for the active site of copper containing nitrite reductase. The 77-K EPR spectrum of CuMe2bpaCl2 in the collagen matrix reveals the typical axial signals of a tetragonal Cu2+ chromophore. The redox potential is -63 mV at pH 5.5. In the presence of nitrite, an increase in the cathodic current is observed in the cyclic voltammogram of CuMe2bpaCl2 in the collagen matrix. Upon reaching -300 mV, a linear generation of NO is observed for the CuMe2bpaCl2/collagen film-coated electrode. The relationship between the rate of NO generation and the nitrite concentration in solution using the Michaelis-Menten equation, results in Vmax 3.16 nM per s and Km 1.1 mM at pH 5.5. The current increase and the reaction rate are dependent on the pH of the solution. The mechanism of nitrite reduction by the copper complex in the collagen matrix is the same mechanism as that of the enzyme in aqueous solution
-
-
-
additional information
?
-
-
study on strucuture-function relationship using copper(I)-nitrite complexes with sterically hindered tris(4-imidazolyl)carbinols such as tris(1-methyl-2-ethyl-4-imidazolyl)carbinol, tris(1-methyl-2-isopropyl-4-imidazolyl)carbinol, or tris(1-pyrazolyl)methanes such as tris(3,5-dimethyl-1-pyrazolyl)methane or tris(3,5-diethyl-1-pyrazolyl)methane, and tris(3,5-diisopropyl-1-pyrazolyl)methane. All of these complexes are good functional models of Cu-NiR that form NO and copper(II) acetate complexes well from reactions with acetic acid under anaerobic conditions. The copper(I) nitrite complex with the tris(1-methyl-2-ethyl-4-imidazolyl)carbinol ligand, which is similar to the highly conserved three-histidine (His)3 ligand environment in the catalytic site of Cu-NiR, has the highest Cu-NiR activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
-
mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
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
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
Pseudomonas stutzeri ZoBell / ATCC 14405
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
G7ZE78
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
G7ZE78
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A085FMZ3
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
M4Z2Q6
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
M4Z2Q6
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A4IL26
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A4IL26
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A090F2L3
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I7ESA1
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I7ESA1
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A2C9EU40
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A2C9EU40
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A021X0B0
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I3X948
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I3X948
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077M3S9
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077M3S9
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077MDD6
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077MDD6
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
cytochrome c550 and pseudoazurin are the alternative electron mediator proteins between the cytochrome bc1 and the cytochrome cd1 type nitrite reductase
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
role in respiration
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
-
reduced azurin + O2
oxidized azurin + H2O
-
putative physiological electron donor
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
-
additional information
?
-
-
cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
-
-
-
additional information
?
-
Q9JYE1
a conserved and functional aniA gene is not essential for meningococcal survival
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome
-
cytochrome c-552 or cytochrome c-553 from Pseudomonas denitrificans acts as acceptor
-
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
-
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
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
-
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
-
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
-
characterization of the nitrosyl d1 heme complex by high-field-pulse electron papramagnetic spectroscopy spectra and derived 14N hyperfine and quadrupole interactions. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution
heme
-
cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer
heme
heme c and heme d1, cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer
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
heme
-
nitrite reductase activitiy of cytochrome c is dependent on the pentacoordination of the heme iron
heme d
-
oxidation-reduction behavior, formation of an oxygenated intermediate at heme d
-
Heme d1
-
the recombinant enzyme, expressed in Pseudomonas putida, contains c-heme but no d1-heme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
Iron
KCl
Molybdenum
nitrite reduction is catalyzed by molybdenum in the active site
Zn
-
the recombinant enzyme, expressed in Pseudomonas putida, contains c-heme but no d1-heme. Reconstitution of this protein with Zn-protoporphyrin IX in the place of the d1-heme. Photoexcitation of Zn-NIR is followed by electron transfer from the triplet excited state of the Zn-porphyrin to the oxidized c-haem. Reduction of the d1-heme is associated with a substantial reorganization of the coordination of the metal
copper
-
blue copper enzyme that shows little absorbance in the 460 nm range, purified recombinant nonactivated enzyme contains 1.97 mol Copper/mol enzyme, the CuSO4 activated enzyme contains 5.97 mol copper/mol enzyme i.e. 6 copper atoms per trimer, CuSO4 activation restores type 2 copper centers which are the sites of catalysis
copper
-
the type 1 Cu center functions as electron acceptor from the physiological electron donor azurin I, the type 2 Cu center is involved in binding and reduction of the substrate
copper
-
enzyme contains type 1 and type 2 copper centers, 6.3 copper atoms per trimer, blue copper enzyme
copper
-
contains 2 type 1 copper atoms per molecule but no other types of copper
copper
ligands of the type 1 and 2 Cu centers are completely conserved in NiR. They are His253, Cys294, His302, and Met307 for the type 1 Cu center and His258, His293, and His456 for type 2.Asp256 and His405 residues are important for enzyme catalysis by forming a hydrogen bond network on the type 2 Cu center. The EPR spectrum is also characteristic of NirK proteins that contain both type 1 and type 2 copper centers
copper
two His nitrogen atoms (His126 and His174), and two sulfur atoms, one from Cys166 and the other from Met179, coordinate the Cu atom
copper
-
blue copper enzyme, 1 type 1 and 1 type 2 Cu atoms per subunit
copper
-
enzyme contains 2 type I copper and 1 type II copper ions
copper
-
2.6 atoms copper per subunit, 2 type 1 Cu and 0.6 type 2 Cu
copper
-
the C-terminal cytochrome c domain is located at the surface of the type 1 copper site in the N-terminal domain from the adjacent subunit. The heme-to-Cu distance of 10.6 A is comparable to the transient electron transfer complex of normal Cu-nitrite reductase with cytochrome c
copper
-
3.2 copper ions per trimer, most probably 3 type 1 and 3 type 2 copper, respectively
copper
-
one subunit contains a type 1 copper center, the second subunit a type 2 copper center, activity of copper depleted enzyme can be restored
copper
-
copper atoms are coordinated by H122, C159, H168, and M173 for the type 1 Cu site and H127, H158, and H321 for the type 2 Cu site. The absorption spectrum of NirK displays two peaks at 598 and 449 nm characteristic for type I Cu proteins
Cu2+
-
each monomer of the trimeric enzyme contains two copper sites: type I (T1) and type II (T2), which are connected via a cysteine (Cys)-histidine (His) bridge for rapid electron transfer. T1 and T2 copper sites structure, PDB ID 2BWD
Cu2+
-
copper-containing dissimilatory nitrite reductase, catalytic type 2 copper, binding site structure, analysis of binding structure and interaction with inhibitors, overview
Cu2+
-
homotrimeric CuNIR contains one type 1 (T1Cu) and one type 2 Cu (T2Cu) site per monomer. The T1Cu atom is coordinated by four amino acid residues (two histidine residues, cysteine and methionine) and functions as a receptor site for the electron supplied by an electron-donor protein such as c-type heme-containing cytochrome or blue-copper proteins. The T2Cu site is a catalytic centre composed of three histidine residues and an axial ligand water molecule. Copper centre structure, overview
Iron
-
nitrite reductase activitiy of cytochrome c is dependent on the pentacoordination of the heme 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tungsten
replacement of molybdenum by tungsten abolishes NO formation
additional information
-
relatively ineffective at 1 mM: CO, bathocuproine, diethyl dithiocarbamate, o-phenanthroline and alpha,alpha'-dipyridyl
-
additional information
-
endogenous inhibitor of nitrite reductase from Pseudomonas aeruginosa: a non-blue copper-containing glycoprotein of 10000 Da that contains 1 atom of EPR-detectable type II copper
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Subtilisin
-
species of 48000 Da which contains the d1 but not the c heme
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
reduced methyl viologen
pH and temperature not specified in the publication
0.035
azurin
-
recombinant wild-type and Y10F mutant enzyme, at pH 6.2 and 27°C
0.00177
cytochrome c551
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
0.0018
cytochrome c551
-
recombinant H327A mutant enzyme, O2 reduction
-
0.0075
cytochrome c551
-
recombinant H369A mutant enzyme, O2 reduction
-
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 cytochrome c550; 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
4.04
nitrite
pH and temperature not specified in the publication
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
-
25°C, pH 7.0, electron donor horse heart cytochrome c; initially oxidized enzyme, electron donor horse heart cytochrome c
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.583
cytochrome c551
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
0.6
cytochrome c551
-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
-
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
0.08
nitrite
-
pH 6.2, 25°C, mutant enzyme H327A; pH 6.2, 25°C, mutant enzyme H369A
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
80
NO2-
-
electron donor: reduced tetramethyl-4-phenylenediamine
106
NO2-
-
all-ferric nitrite-bound complex, electron donor pseudoazurin
0.11
O2
-
25°C, pH 7.0, electron donor horse heart cytochrome c; initially oxidized enzyme, electron donor horse heart cytochrome c
0.17
O2
-
25°C, pH 7.0, electron donor cytochrome c550; initially oxidized enzyme, electron donor cytochrome c550
2.8
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c; pre-reduced enzyme, electron donor horse heart cytochrome c
3
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550; pre-reduced enzyme, electron donor cytochrome c550
6.4
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin; pre-reduced enzyme, electron donor pseudoazurin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.8
-
recombinant enzyme, without activation, enzyme has only type 1 copper centers
22.7
-
enzyme is activated 2.5-4.5fold by freezing at -20°C for 6 h and subsequent thawing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 5.4
-
hydroxylamine reduction, electron donor pseudoazurin, pre-reduced cytochrome cd1; NH2OH reduction, electron donor pseudoazurin
5.4
-
hydroxylamine reduction, electron donor cytochrome c550, pre-reduced cytochrome cd1; NH2OH reduction, electron donor cytochrome c550
5.7
-
nitrite reduction, electron donor cytochrome c550; nitrite reduction, electron donor cytochrome c550, pre-reduced cytochrome cd1
5.8
-
nitrite reduction, electron donor pseudoazurin; nitrite reduction, electron donor pseudoazurin, pre-reduced cytochrome cd1
6.2
-
O2 reduction, electron donor cytochrome c550; O2 reduction, electron donor cytochrome c550, pre-reduced cytochrome cd1
6.3
-
O2 reduction, electron donor pseudoazurin; O2 reduction, electron donor pseudoazurin, pre-reduced cytochrome cd1
6.5
6.5 - 7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9 - 6.2
-
pH 4.9: about 55% of maximal ativity, pH 6.2: about 65% of maximal activity, reaction with 0.5 mM nitrite and pseudoazurin as electron donor
5.2 - 6.5
-
pH 5.2: about 60% of maximal activity, pH 6.5: about 55% of maximal activity, reaction with 5 mM nitrite and pseudoazurin as electron donor
7.5
3fold decrease in the rate of NO formation compared to pH 6.5; 3fold decrease in the rate of NO formation compared to pH 6.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 80
60°C: about 60% of maximal activity, 80°C: about 90% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
storage at -20°C for several months leads to an increase in the number of isoelectrophoretic forms. All preparations have two primary bands, one with a pI of 6.97 and the other of 7.02. Both bands possess significant cytochrome oxidase activity after elution from the gels. When each of the primary bands is eluted and again subject to isoelectric focusing under the same conditions as before, each band interconverts into two bands with pIs of 6.97 and 7.02
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the enzyme is synthesized exclusively in
-
the enzyme is synthesized exclusively in
additional information
-
enzyme is released from bacteria, after exposure to different antimicrobial agents
additional information
-
enzyme is released from bacteria, after exposure to different antimicrobial agents
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
important differences in the primary structure of the cytoplasmic enzyme form and the extracellularv enzyme form, indicating that Haloferax mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Haloferax mediterranei sequence indicate that these processes are closely related to the Tat system
-
important differences in the primary structure of the cytoplasmic enzyme form and the extracellularv enzyme form, indicating that Haloferax mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Haloferax mediterranei sequence indicate that these processes are closely related to the Tat system
-
important differences in the primary structure of the cytoplasmic enzyme form and the extracellularv enzyme form, indicating that Haloferax mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Haloferax mediterranei sequence indicate that these processes are closely related to the Tat system
-
-
important differences in the primary structure of the cytoplasmic enzyme form and the extracellularv enzyme form, indicating that Haloferax mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Haloferax mediterranei sequence indicate that these processes are closely related to the Tat system
-
-
-
enzyme is released from bacteria, after exposure to different antimicrobial agents
-
-
enzyme is released from bacteria, after exposure to different antimicrobial agents
-
-
-
equally distributed between the soluble- and the membrane fraction
the first 65 amino acid residues of theN-terminal domain constitute a mitochondrial targeting signal, sequence analysis
-
75% of enzyme activity found in the soluble fraction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT