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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms menaquinol:no oxidoreductase, menaquinol-dependent nitric oxide reductase, more
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menaquinol-dependent nitric oxide reductase
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menaquinol:NO oxidoreductase
menaquinol NO reductase
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menaquinol NO reductase
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menaquinol:NO oxidoreductase
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menaquinol:NO oxidoreductase
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2 nitric oxide + menaquinol = nitrous oxide + menaquinone + H2O
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MetaCyc
nitrate reduction VII (denitrification)
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nitric oxide + ascorbic acid
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nitric oxide + cytochrome c551
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nitric oxide + juglone
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Substrates: - Products: -
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nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
nitric oxide + plumbagin
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Substrates: - Products: -
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NO + menaquinol
N2O + H2O + menaquinone
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Substrates: - Products: -
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additional information
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nitric oxide + ascorbic acid
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Substrates: - Products: -
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nitric oxide + ascorbic acid
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Substrates: - Products: -
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nitric oxide + cytochrome c551
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Substrates: - Products: -
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nitric oxide + cytochrome c551
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Substrates: the menaquinol pathway has a 4fold greater maximal activity than the pathway via cytochrome c551 Products: -
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nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
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Substrates: - Products: -
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nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
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Substrates: highest activity with menaquinol Products: -
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nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
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Substrates: the menaquinol pathway has a 4fold greater maximal activity than the pathway via cytochrome c551 Products: -
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nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
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Substrates: highest activity with menaquinol Products: -
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additional information
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Substrates: no activity with horse heart ferrocytochrome c Products: -
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additional information
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Substrates: no activity with lapachol, reduced horse heart cytochrome c, cytochrome c550, and cytochrome c552 Products: -
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additional information
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Substrates: the activity using sodium borohydride-reduced menaquinone is about 2times higher than obtained in the presence of ascorbic acid, phenazine methosulfate, and horse heart cytochrome c Products: -
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additional information
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Substrates: the bifunctional qCuANOR can accept electrons from two donors, a specific cytochrome c551 and menaquinol Products: -
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additional information
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Substrates: no activity with horse heart ferrocytochrome c Products: -
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additional information
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Substrates: the activity using sodium borohydride-reduced menaquinone is about 2times higher than obtained in the presence of ascorbic acid, phenazine methosulfate, and horse heart cytochrome c Products: -
?
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NO + menaquinol
N2O + H2O + menaquinone
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Substrates: - Products: -
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heme
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heme
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the enzyme contains two b-type hemes per enzyme complex. The heme b content of the purified NO reductase is 25.7 nmol/mg. Heme c is absent
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copper
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the enzyme contains a CuA center in its small subunit
Cu2+
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copper A containing enzyme with two copper atoms per enzyme complex, the copper content is 26.7 nmol/mg of protein
Cu2+
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qCuANOR is a member of the heme-copper oxidase superfamily
Iron
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qNOR contains two heme iron and one nonheme iron
Iron
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the enzyme contains one non-heme iron per enzyme complex. The non-heme iron content is 13.7 nmol/mg
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cytochrome c551
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noncompetitive inhibitor of nitric oxide reduction when menaquinol is used as an electron donor
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NO
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substrate inhibition at high concentratins
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ferricytochrome c
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NOR activity is stimulated by ferrocytochrome c when phenazine methosulfate and ascorbate are both present
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0.0045
cytochrome c551
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pH and temperature not specified in the publication
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0.141
juglone
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pH and temperature not specified in the publication
0.256
Plumbagin
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pH and temperature not specified in the publication
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41
nitric oxide
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using cytochrome c551 as electron donor, pH and temperature not specified in the publication
118
nitric oxide
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using juglone as electron donor, pH and temperature not specified in the publication
150
nitric oxide
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using plumbagin as electron donor, pH and temperature not specified in the publication
153
nitric oxide
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using menaquinol as electron donor, pH and temperature not specified in the publication
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0.007
NO
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54.5°C, pH 7.0, qNOR in membrane
0.015
NO
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54.5°C, pH 7.0, purified qNOR
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0.67
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crude membrane extract, pH and temperature not specified in the publication
40.7
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after 60.5fold purification, pH and temperature not specified in the publication
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4 - 10
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approx. 50% of maximal activity at pH 5.0, almost no activity at pH 10.0
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25 - 93
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no activity detectable below 25°C
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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physiological function
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the ability of qCuANOR to accept electrons from both menaquinol and cytochrome c551 may be related to the regulation of the rate of NO reduction especially as a defense mechanism of B. azotoformans against the toxicity of NO. The menaquinol pathway, which has a 4-fold greater maximal activity than the pathway via cytochrome c551, is used for NO detoxification, whereas electron donation via the endogenous cytochrome c involves the cytochrome b6f complex serving the bioenergetic needs of the organism
physiological function
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the menaquinol-linked pathway is involved in the detoxification of nitric oxide
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X4Y370_9BACT
131
4
14978
TrEMBL
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X4Y361_9BACT
130
4
14847
TrEMBL
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X4Y5Y5_9BACT
134
4
15367
TrEMBL
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X4Y5Y1_9BACT
130
4
14897
TrEMBL
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X4YJ39_9BACT
134
4
15458
TrEMBL
-
X4YKU9_9BACT
133
4
15238
TrEMBL
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X4XWP4_9BACT
131
4
15107
TrEMBL
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X4YKV2_9BACT
134
4
15397
TrEMBL
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X4Y5Z2_9BACT
131
4
14951
TrEMBL
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A7GXN1_CAMC5
Campylobacter curvus (strain 525.92)
746
14
83666
TrEMBL
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X4YKU2_9BACT
131
4
15075
TrEMBL
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A0A0M4STY5_9PROT
743
14
83548
TrEMBL
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X4YJ50_9BACT
134
4
15383
TrEMBL
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L0NKL6_9HYPH
447
12
50505
TrEMBL
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X4Y373_9BACT
133
4
15254
TrEMBL
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A0A7D3V6H8_9PROT
746
14
83678
TrEMBL
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A7ZCA5_CAMC1
Campylobacter concisus (strain 13826)
743
14
83592
TrEMBL
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X4YJ44_9BACT
127
4
14502
TrEMBL
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X4YKU4_9BACT
134
4
15475
TrEMBL
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X4YJ48_9BACT
128
4
14658
TrEMBL
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16000
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1 * 16000 + 1 * 40000, SDS-PAGE
40000
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1 * 16000 + 1 * 40000, SDS-PAGE
78800
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1 * 78800, deduced from nucleotide sequence
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heterodimer
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1 * 16000 + 1 * 40000, SDS-PAGE
heterodimer
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1 * 16000 + 1 * 40000, SDS-PAGE
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monomer
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1 * 75000-80000, SDS-PAGE, assuming that qNOR binds one dodecyl maltoside micelle of about 40000-50000 Da
monomer
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1 * 78800, deduced from nucleotide sequence
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25
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no loss of activity after 24 h, qNOR in membrane
56
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50% loss of activity after 630 min, qNOR in membrane
75
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50% loss of activity after 231 min, qNOR in membrane
100
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50% loss of activity after 4 min, purified qNOR
100
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50% loss of activity after 86 min, qNOR in membrane
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1% dodecyl maltoside, CM-Sepharose, hydroxyapatite
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Q-Sepharose column chromatography, Sephadex G25 gel filtration, and Bio-Scale Ceramic CHT20-I hydroxyapatite column chromatography
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Suharti; Heering, H.A.; de Vries, S.
NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551
Biochemistry
43
13487-13495
2004
Schinkia azotoformans
brenda
de Vries, S.; Strampraad, M.J.; Lu, S.; Moenne-Loccoz, P.; Schroder, I.
Purification and characterization of the MQH2:NO oxidoreductase from the hyperthermophilic archaeon Pyrobaculum aerophilum
J. Biol. Chem.
278
35861-35868
2003
Pyrobaculum aerophilum
brenda
Suharti, S.; de Vries, S.
Membrane-bound denitrification in the Gram-positive bacterium Bacillus azotoformans
Biochem. Soc. Trans.
33
130-133
2005
Schinkia azotoformans
brenda
Suhart, S.; Strampraad, M.; Schrder, I.; De Vries, S.
A novel copper A containing menaquinol NO reductase from Bacillus azotoformans
Biochemistry
40
2632-2639
2001
Schinkia azotoformans, Schinkia azotoformans NCCB 100003
brenda
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