Information on EC 1.7.2.1 - nitrite reductase (NO-forming)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.7.2.1
-
RECOMMENDED NAME
GeneOntology No.
nitrite reductase (NO-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ammonia oxidation II (anaerobic)
-
-
Microbial metabolism in diverse environments
-
-
nitrate reduction I (denitrification)
-
-
nitrate reduction VII (denitrification)
-
-
nitrifier denitrification
-
-
nitrite-dependent anaerobic methane oxidation
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Nitrogen metabolism
-
-
denitrification
-
-
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 hide
9027-00-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NCIB 11015
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain TK-6
SwissProt
Manually annotated by BRENDA team
strain TK-6
SwissProt
Manually annotated by BRENDA team
formerly Aquaspirillum magnetotacticum
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild-type strain MC58, gene nitrite reductase aniA
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 5276
-
-
Manually annotated by BRENDA team
DSM 50135
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferrocytochrome c + O2
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
show the reaction diagram
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
show the reaction diagram
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
show the reaction diagram
hydroxylamine + reduced pseudoazurin
NH3 + H2O + oxidized pseudoazurin
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + oxidized benzyl viologen
?
show the reaction diagram
-
-
-
-
?
NH2OH + NaNO2
N2O + H2O
show the reaction diagram
-
-
-
?
NH2OH + reduced cytochrome c550
NH3 + H2O + oxidized cytochrome c550
show the reaction diagram
-
additional electron donor: horse heart cytochrome c
-
?
nitrite + dithionite
NO + reduced dithionite
show the reaction diagram
-
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 + electron donor
NO + oxidized electron donor
show the reaction diagram
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
show the reaction diagram
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
show the reaction diagram
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
show the reaction diagram
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
show the reaction diagram
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
show the reaction diagram
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
show the reaction diagram
-
-
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
show the reaction diagram
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
show the reaction diagram
-
anaerobic assay conditions
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
show the reaction diagram
nitrite + methyl viologen
NO + oxidized methyl viologen + H2O
show the reaction diagram
-
-
-
?
nitrite + reduced azurin
NO + H2O + oxidized azurin
show the reaction diagram
nitrite + reduced azurin
NO + oxidized azurin
show the reaction diagram
-
azurin purified from Pseudomonas chlororaphis
-
-
?
nitrite + reduced azurin I
NO + azurin I
show the reaction diagram
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
show the reaction diagram
nitrite + reduced benzyl viologen
nitric oxide + oxidized benzyl viologen
show the reaction diagram
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
show the reaction diagram
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
show the reaction diagram
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
show the reaction diagram
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
show the reaction diagram
nitrite + reduced methyl viologen
NO + oxidized methyl viologen
show the reaction diagram
-
random sequential mechanism
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
show the reaction diagram
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
show the reaction diagram
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
show the reaction diagram
NO2 + reduced methyl viologen
NO + oxidized methylviologen
show the reaction diagram
-
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
show the reaction diagram
NO2- + morpholine
N-nitrosomorpholine
show the reaction diagram
-
in the presence of diethyldithiocarbamic acid ethylester, nitrosation through the production of NO or NO+-like species
-
?
NO2- + Na2S2O4
NO + Na2S2O3
show the reaction diagram
-
pysiological electron donor is unknown, no activity with methyl viologen, phenazine methosulfate or N,N,N',N',-tetramethyl-p-phenylenediamine
-
?
NO2- + reduced ascorbate
NO + oxidized ascorbate
show the reaction diagram
NO2- + reduced azurin
NO + oxidized azurin
show the reaction diagram
-
putative physiological electron donor
-
?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
show the reaction diagram
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
show the reaction diagram
O2 + ferrocytochrome c
H2O + ferricytochrome c
show the reaction diagram
O2 + reduced pseudoazurin
H2O + oxidized pseudoazurin
show the reaction diagram
-
-
-
-
?
O2-. + H+
H2O2 + O2
show the reaction diagram
-
purified enzyme shows superoxide dismutase activity, approx. one-third that of pure superoxide dismutase
-
-
reduced azurin + O2
oxidized azurin + H2O
show the reaction diagram
reduced tetramethyl-4-phenylenediamine + NO2
oxidized tetrametyl-4-phenylenediamine + NO
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
show the reaction diagram
-
-
-
-
nitrite + electron donor
NO + oxidized electron donor
show the reaction diagram
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
show the reaction diagram
-
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 + ferrocytochrome c
NO + H2O + ferricytochrome c
show the reaction diagram
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
show the reaction diagram
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
show the reaction diagram
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
show the reaction diagram
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
show the reaction diagram
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
show the reaction diagram
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
show the reaction diagram
NO2- + ferrocytochrome c
NO + ferricytochrome c
show the reaction diagram
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
show the reaction diagram
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
show the reaction diagram
-
unambiguously identified as physiological electron donor
-
?
reduced azurin + O2
oxidized azurin + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
-
cytochrome cd1
-
heme c
heme d
-
Heme d1
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
copper-containing dissimilatory nitrite reductase, catalytic type 2 copper, binding site structure, analysis of binding structure and interaction with inhibitors, overview
LiCl
-
2 M, enzyme is activated by high salt concentrations
NaCl
optimum salt concentration: 2 M
NaNO3
-
2 M, enzyme is activated by high salt concentrations
NH4Cl
-
2 M, enzyme is activated by high salt concentrations
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
Zn2+
-
present on surface of each monomer, crystallization data
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
-
weak, mixed-type inhibition, inhibition mode, overview
azide
-
binding mode, overview
CO
20% residual activity
diethyldithiocarbamate
formate
-
weak mixed-type inhibition, inhibition mode, overview
methylhydrazine
-
irreversible
NaN3
-
1 mM, 60% inhibition
NH2OH
-
1 mM, 50% inhibition
nitrate
-
weak inhibition, inhibition mode, overview
Nitrous oxide
-
binding mode, overview
Oxidized cytochrome c
-
-
-
phenylhydrazine
-
irreversible
Urea
-
4 M, 60% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NapC
-
c-type cytochrome with 4 bis-histidinyl coordinated hemes capable of reducing and hence activating oxidized cytochrome cd1 nitrite reductase
-
Subtilisin
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species of 48000 Da which contains the d1 but not the c heme
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00084 - 0.049
azurin
0.0305 - 0.046
cytochrome c
0.00177 - 0.0075
cytochrome c551
-
0.0018 - 0.0075
Ferrocytochrome c-551
-
0.43 - 2.5
hydroxylamine
0.434 - 2.5
NH2OH
0.00008 - 416
nitrite
0.00147 - 0.8
NO2-
0.027 - 1
O2
0.067 - 0.16
pseudoazurin
-
0.41
reduced methyl viologen
pH and temperature not specified in the publication
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
Abz-VAA
Pseudomonas aeruginosa
-
25°C, pH 6.9, recombinant enzyme
-
1 - 3.2
azurin
1.33
cytochrome c
Pseudomonas aeruginosa
-
succinylated monomeric enzyme
0.583 - 2.8
cytochrome c551
-
0.025 - 0.043
Ferrocytochrome c-551
-
5
ferrocytochrome c2
Rhodobacter sphaeroides
-
-
0.1
ferrocytochrome V(gamma)
Rhodobacter sphaeroides
-
-
-
0.08 - 7.7
hydroxylamine
0.08 - 6.4
NH2OH
0.08 - 1478
nitrite
38 - 125
NO
0.08 - 144
NO2-
0.11 - 6.4
O2
additional information
additional information
Achromobacter cycloclastes
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
azide
-
recombinant enzyme, pH 6.5, 25°C
0.0049
oxidized azurin
-
-
-
0.001 - 0.002
oxidized cytochrome b551
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.048
-
nitrite reduction
0.33
-
electron donor azurin
2.1
-
nitrite reduction, elctron donor methyl viologen
3.32
-
reduction of N,N,N',N'-tetramethyl-4-phenyldiamine
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
40
-
if reduced nitrite is measured
45.2
-
native recombinant enzyme, azurin
80 - 90
-
if oxidized benzyl viologen is measured
82
-
mutant N90S, pH 7.1
107
-
native recombinant enzyme, dithionite
117
-
after storage at -20°C for 25 h and thawing in a water bath at 20°C
123
-
mutant H254F, pH 7.1
130
-
electron donor benzyl viologen
167.7
-
recombinant enzyme, after activation with CuSO4
168
-
native recombinant enzyme, methyl viologen
240
-
wild-type, pH 7.1
303
pH 6.5, 35°C
960
-
in the presence of 2 M NaCl
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6.5
-
assay at, pH dependence, overview
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
5.6
-
reaction with 0.5 mM nitrite and pseudoazurin as electron donor
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
optimum below pH 6.5
6.5 - 7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
almost no activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 80
60°C: about 60% of maximal activity, 80°C: about 90% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 6.2
-
isoelectric focusing
9.3
isoelectric focusing
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
MLTC-1
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the first 65 amino acid residues of theN-terminal domain constitute a mitochondrial targeting signal, sequence analysis
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Geobacillus kaustophilus (strain HTA426)
Geobacillus kaustophilus (strain HTA426)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Ralstonia pickettii (strain 12J)
Ralstonia pickettii (strain 12J)
Ralstonia pickettii (strain 12J)
Ralstonia pickettii (strain 12J)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36500
-
3 * 36500, calculated from sequence, crystal structure
37700
-
3 * 37700, SDS-PAGE
39800
3 * 39800, SDS-PAGE, intracellular enzyme
41800
-
2 * 41800, SDS-PAGE
44300
3 * 44300, SDS-PAGE, extracellular enzyme
46000
-
3 * 46000, SDS-PAGE
53705
x * 53705, calculated, x * 60000, SDS-PAGE
54000
-
2 * 54000, SDS-PAGE
60204
-
2 * 60204, deduced from amino acid sequence
61500
1 * 61500, SDS-PAGE
63022
-
2 * 63022, electrospray mass spectroscopy
64000
-
2 * 64000, SDS-PAGE
66000
-
2 * 66000, SDS-PAGE
69000
-
gel filtration
70000
-
gel filtration
80000
-
gel filtration, gradient PAGE
83300
-
gel filtration
100000
-
gel filtration
103000
105000
-
sedimentation equlibrium
107000
-
gel filtration
113000
-
gel filtration
127000
-
gel filtration
130000
-
gel filtration
131000
-
gel filtration
133000
-
gel filtration
167000
-
gel filtration
400000
-
gel filtration
900000
gel filtration, aggregate