1.7.2.1: nitrite reductase (NO-forming)
This is an abbreviated version!
For detailed information about nitrite reductase (NO-forming), go to the full flat file.
Word Map on EC 1.7.2.1
-
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
- 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
Reaction
Synonyms
AcNIR, AfNiR, AniA, AxNiR, BRAO375_2740002, C551-O2 oxidoreductase, cd1 nitrite reductase, cd1NiR, cNOR, copper-containing dissimilatory nitrite reductase, copper-containing nitrite reductase, Cu-NIR, Cu-NirK, CuNIR, cytochrome c-551:O2, NO2- oxidoreductase, cytochrome cd, cytochrome cd1 nitrite reductase, cytochrome oxidase, dissimilatory nitrite reductase, dissimilatory nitrite reductase cytochrome cd1, EC 1.6.6.5, EC 1.7.99.3, EC 1.9.3.2, GK0767, GtNiR, HdNIR, hemoglobin, HydNIR, HYPDE_25578, KSU1_D0929, mARC1, mARC2, mitochondrial amidoxime reducing component, MRA2164, NiR, NiR-Pa, NirK, NirS, nitrite reductase, oxidase, Pseudomonas cytochrome, PaNiR, PNR, Pseudomonas cytochrome oxidase, PsNiR, reductase, nitrite (cytochrome), Rpic_4015, S58_68210
ECTree
1.7.2.1 nitrite reductase (NO-forming)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.7.2.1 - nitrite reductase (NO-forming)
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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+
Marinobacter nauticus
-
-
-
-
?
nitric oxide + H2O + ferricytochrome c B0428
nitrite + ferrocytochrome c B0428 + 2 H+
-
-
-
?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + 2 H+
-
-
-
?
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
Marinobacter nauticus
-
-
-
-
?
nitric oxide + H2O + oxidized phenazine methosulfate
nitrite + reduced phenazine methosulfate + 2 H+
Marinobacter nauticus
-
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+
Marinobacter nauticus
-
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 + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
-
-
-
-
?
nitrite + ferrocytochrome V(gamma) + H+
nitric oxide + H2O + ferricytochrome V(gamma)
-
-
-
-
r
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
anaerobic assay conditions
-
-
?
nitrite + methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced ascorbate
nitric oxide + oxidized ascorbate
-
-
-
-
r
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
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
-
-
-
r
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
-
artificial electron donor: reduced benzyl viologen
-
?
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
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
Nitrososphaera viennensis JCM19564
-
-
-
-
?
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 c2
NO + H2O + ferricytochrome c2
-
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 benzyl viologen
NO + oxidized benzyl viologen
-
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen + 2 H+
nitric oxide + H2O + oxidized benzyl viologen
-
-
-
?
nitrite + reduced benzyl viologen + 2 H+
nitric oxide + H2O + oxidized benzyl viologen
Nitrososphaera viennensis JCM19564
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
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 phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
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
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
random sequential mechanism
-
-
?
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
-
-
?
nitrite + reduced pseudoazurin + H+
nitric oxide + oxidized pseudoazurin + H2O
-
-
-
-
r
nitrite + reduced pseudoazurin + H+
nitric oxide + oxidized pseudoazurin + H2O
-
-
-
-
r
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
?
-
-
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
?
-
-
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
?
-
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
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
?
-
-
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
?
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spectroscopic analysis of the reactivity of cd1NiR and its semi-apo derivative with NO. The c heme nitrosylation is enhanced during catalysis
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nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
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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
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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
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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
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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
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study on structure-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
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