BRENDA - Enzyme Database
show all sequences of 1.7.2.6

Reduction of nitric oxide catalyzed by hydroxylamine oxidoreductase from an anammox bacterium

Irisa, T.; Hira, D.; Furukawa, K.; Fujii, T.; J. Biosci. Bioeng. 118, 616-621 (2014)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
quasi steady-state and steady-state kinetics, kinetic analysis, overview
Candidatus Kuenenia stuttgartiensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
hydroxylamine + H2O + 4 ferricytochrome c
Candidatus Kuenenia stuttgartiensis
via NO as intermediate
nitrite + 4 ferrocytochrome c + 5 H+
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
Candidatus Kuenenia stuttgartiensis KSU-1
via NO as intermediate
nitrite + 4 ferrocytochrome c + 5 H+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Candidatus Kuenenia stuttgartiensis
-
-
-
Candidatus Kuenenia stuttgartiensis KSU-1
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
hydroxylamine + H2O + 4 ferricytochrome c
via NO as intermediate
742931
Candidatus Kuenenia stuttgartiensis
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
via NO as intermediate
742931
Candidatus Kuenenia stuttgartiensis KSU-1
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
r
hydroxylamine + H2O + benzylviologen
-
742931
Candidatus Kuenenia stuttgartiensis
NO + reduced benzylviologen + 2 H+
-
-
-
?
hydroxylamine + H2O + benzylviologen
-
742931
Candidatus Kuenenia stuttgartiensis KSU-1
NO + reduced benzylviologen + 2 H+
-
-
-
?
hydroxylamine + H2O + methylviologen
-
742931
Candidatus Kuenenia stuttgartiensis
NO + reduced methylviologen + 2 H+
-
-
-
?
hydroxylamine + H2O + methylviologen
-
742931
Candidatus Kuenenia stuttgartiensis KSU-1
NO + reduced methylviologen + 2 H+
-
-
-
?
additional information
enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview
742931
Candidatus Kuenenia stuttgartiensis
?
-
-
-
?
additional information
enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview
742931
Candidatus Kuenenia stuttgartiensis KSU-1
?
-
-
-
?
NO + ferrocytochrome c + 2 H+
-
742931
Candidatus Kuenenia stuttgartiensis
hydroxylamine + H2O + ferricytochrome c
-
-
-
r
NO + ferrocytochrome c + 2 H+
-
742931
Candidatus Kuenenia stuttgartiensis KSU-1
hydroxylamine + H2O + ferricytochrome c
-
-
-
r
NO + H2O + ferricytochrome c
-
742931
Candidatus Kuenenia stuttgartiensis
nitrite + ferrocytochrome c + 2 H+
-
-
-
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
assay at
Candidatus Kuenenia stuttgartiensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Candidatus Kuenenia stuttgartiensis
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c
-
Candidatus Kuenenia stuttgartiensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c
-
Candidatus Kuenenia stuttgartiensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
quasi steady-state and steady-state kinetics, kinetic analysis, overview
Candidatus Kuenenia stuttgartiensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
hydroxylamine + H2O + 4 ferricytochrome c
Candidatus Kuenenia stuttgartiensis
via NO as intermediate
nitrite + 4 ferrocytochrome c + 5 H+
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
Candidatus Kuenenia stuttgartiensis KSU-1
via NO as intermediate
nitrite + 4 ferrocytochrome c + 5 H+
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
hydroxylamine + H2O + 4 ferricytochrome c
via NO as intermediate
742931
Candidatus Kuenenia stuttgartiensis
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
via NO as intermediate
742931
Candidatus Kuenenia stuttgartiensis KSU-1
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
r
hydroxylamine + H2O + benzylviologen
-
742931
Candidatus Kuenenia stuttgartiensis
NO + reduced benzylviologen + 2 H+
-
-
-
?
hydroxylamine + H2O + benzylviologen
-
742931
Candidatus Kuenenia stuttgartiensis KSU-1
NO + reduced benzylviologen + 2 H+
-
-
-
?
hydroxylamine + H2O + methylviologen
-
742931
Candidatus Kuenenia stuttgartiensis
NO + reduced methylviologen + 2 H+
-
-
-
?
hydroxylamine + H2O + methylviologen
-
742931
Candidatus Kuenenia stuttgartiensis KSU-1
NO + reduced methylviologen + 2 H+
-
-
-
?
additional information
enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview
742931
Candidatus Kuenenia stuttgartiensis
?
-
-
-
?
additional information
enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview
742931
Candidatus Kuenenia stuttgartiensis KSU-1
?
-
-
-
?
NO + ferrocytochrome c + 2 H+
-
742931
Candidatus Kuenenia stuttgartiensis
hydroxylamine + H2O + ferricytochrome c
-
-
-
r
NO + ferrocytochrome c + 2 H+
-
742931
Candidatus Kuenenia stuttgartiensis KSU-1
hydroxylamine + H2O + ferricytochrome c
-
-
-
r
NO + H2O + ferricytochrome c
-
742931
Candidatus Kuenenia stuttgartiensis
nitrite + ferrocytochrome c + 2 H+
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
assay at
Candidatus Kuenenia stuttgartiensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Candidatus Kuenenia stuttgartiensis
General Information
General Information
Commentary
Organism
physiological function
the anammox HAO can catalyze the interconversion of NO and NH2OH. The anammox HAO functions to adjust anammox by inter-conversion of NO and NH2OH depending on the redox potential of the physiological electron transfer protein in anammox bacteria
Candidatus Kuenenia stuttgartiensis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the anammox HAO can catalyze the interconversion of NO and NH2OH. The anammox HAO functions to adjust anammox by inter-conversion of NO and NH2OH depending on the redox potential of the physiological electron transfer protein in anammox bacteria
Candidatus Kuenenia stuttgartiensis
Other publictions for EC 1.7.2.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743303
Haase
Epsilonproteobacterial hydrox ...
Campylobacter fetus, Caminibacter mediatlanticus, Nautilia profundicola, Campylobacter curvus
Mol. Microbiol.
105
127-138
2017
-
-
4
-
3
-
-
12
-
-
-
-
-
4
-
-
-
-
-
-
8
-
16
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
3
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
8
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741829
Nishigaya
Optimized inhibition assays r ...
Nitrosospira multiformis, Nitrosococcus oceani, Nitrosomonas sp. JPCCT2, Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718, Nitrosococcus oceani ATCC 19707
Biochem. Biophys. Res. Commun.
476
127-133
2016
4
-
4
1
-
-
8
-
-
4
-
6
-
17
-
-
2
-
-
-
-
-
18
-
10
4
-
-
-
4
-
-
8
-
-
4
4
-
4
8
1
-
-
4
8
-
-
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4
-
6
-
-
-
2
-
-
-
-
18
-
4
-
-
-
4
-
-
-
-
-
-
-
-
-
742931
Irisa
Reduction of nitric oxide cat ...
Candidatus Kuenenia stuttgartiensis, Candidatus Kuenenia stuttgartiensis KSU-1
J. Biosci. Bioeng.
118
616-621
2014
-
-
-
-
-
-
-
1
-
-
-
2
-
2
-
-
-
-
-
-
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11
-
-
1
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-
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1
-
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1
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1
-
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-
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1
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2
-
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-
-
-
-
-
11
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
724393
Cedervall
Structural studies of hydroxyl ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Biochemistry
52
6211-6218
2013
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
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-
-
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-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725301
Keluskar
Evaluation of hydroxylamine ox ...
Nitrosomonas europaea
J. Basic Microbiol.
54
261-268
2013
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
711263
Kostera
Enzymatic interconversion of a ...
Nitrosomonas europaea
Biochemistry
49
8546-8553
2010
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
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5
-
1
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1
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1
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5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725885
Hozuki
Effect of salinity on hydroxyl ...
Nitrosococcus oceani, Nitrosococcus oceani NS58
Microbes Environ.
25
95-102
2010
-
-
-
-
-
-
-
2
-
-
1
-
-
2
-
-
1
-
-
-
-
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4
2
-
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2
-
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2
-
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-
2
-
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-
-
-
-
2
-
-
1
-
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1
-
-
-
-
4
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
696882
Radniecki
Expression of merA, trxA, amoA ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Biotechnol. Bioeng.
104
1004-1011
2009
-
-
-
-
-
-
2
-
-
-
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2
-
5
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2
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1
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2
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2
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2
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-
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-
-
-
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-
710728
Cedervall
Crystallization and preliminar ...
Nitrosomonas europaea
Acta Crystallogr. Sect. F
65
1296-1298
2009
-
-
-
2
-
-
-
-
-
-
1
1
-
1
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2
-
-
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1
2
2
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2
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2
2
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1
1
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2
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-
1
2
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-
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-
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-
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-
-
-
-
674203
Pulcu
Direct electrochemistry of tet ...
Nitrosomonas europaea
J. Am. Chem. Soc.
129
1838-1839
2007
-
-
-
-
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1
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1
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1
1
2
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2
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1
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1
1
-
-
-
-
-
-
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-
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-
-
-
672673
Hirota
Transcriptional analysis of th ...
Nitrosomonas sp., Nitrosomonas sp. ENI-11
Biosci. Biotechnol. Biochem.
70
1875-1881
2006
-
-
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-
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1
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3
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1
2
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1
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1
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-
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-
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-
-
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-
658903
Cabail
Laser photoinitiated nitrosyla ...
Nitrosomonas europaea
Inorg. Chem.
44
225-231
2005
-
-
-
-
-
-
-
-
-
1
1
1
-
1
-
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1
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1
1
1
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3
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3
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1
1
1
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1
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1
1
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672015
Kurnikov
Redox equilibria in hydroxylam ...
Nitrosomonas europaea
Biochemistry
44
1856-1863
2005
-
-
-
-
-
-
-
-
-
-
-
-
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1
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1
1
2
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1
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1
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-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656327
Tokuyama
Nitrosomonas communis strain Y ...
Nitrosomonas europaea, Nitrosomonas sp. K1, Nitrosomonas communis, Nitrosomonas communis YNSRA
J. Biosci. Bioeng.
98
309-312
2004
-
-
-
-
-
-
-
-
-
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4
-
-
-
-
-
-
3
-
4
-
6
3
-
-
-
3
-
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3
-
4
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3
-
-
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3
-
-
-
-
-
-
-
-
-
658900
Cabail
Selective one-electron reducti ...
Nitrosomonas europaea
Inorg. Chem.
42
270-272
2003
-
-
-
-
-
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2
1
-
1
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1
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3
2
2
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3
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3
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2
1
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1
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3
2
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657688
Arp
Molecular biology and biochemi ...
Nitrosomonas europaea
Arch. Microbiol.
178
250-255
2002
-
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1
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1
1
1
1
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1
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The roles of the three gene co ...
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657930
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Spectroscopic characterization ...
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Biochemistry
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Correlations of structure and ...
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J. Am. Chem. Soc.
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394346
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Mutational analysis of the mul ...
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394335
Arciero
Correlation of optical and EPR ...
Nitrosomonas europaea
Biochemistry
37
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1998
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Effect of ammonia starvation o ...
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720525
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The 2.8 A structure of hydroxy ...
Nitrosomonas europaea
Nat. Struct. Biol.
4
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1997
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Mutagenesis of hydroxylamine o ...
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394341
Logan
Suicide Inactivation of Hydrox ...
Nitrosomonas europaea
Biochemistry
34
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1995
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639387
Logan
Reaction with cyanide of hydro ...
Nitrosomonas europaea
Biochemistry
34
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1995
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Zahn
Oxidation of hydroxylamine by ...
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719635
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The active site of hydroxylami ...
Nitrosomonas europaea, Nitrosomonas europaea Schmidt
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Hydroxylamine oxidoreductase f ...
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Collins
Optical spectropotentiometric ...
Nitrosomonas europaea
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718820
Hooper
Spectroscopic and rapid kineti ...
Nitrosomonas europaea
Biochemistry
30
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394332
Numata
Cytochrome p-460 of Nitrosomon ...
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394316
Tatsuaki
-
Cloning and expression of the ...
Nitrosomonas europaea
Hakko Kogaku Kaishi
66
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1988
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394317
Balny
Effect of solvent, pressure an ...
Nitrosomonas europaea
Eur. J. Biochem.
176
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1988
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394318
Prince
-
Resolution of the hemes of hyd ...
Nitrosomonas europaea
Biochemistry
26
970-974
1987
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394331
Nasri
-
Synthesis and characterization ...
Nitrosomonas europaea
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1987
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394348
DiSpirito
-
A 'blue' copper oxidase from N ...
Nitrosomonas europaea
Biochim. Biophys. Acta
827
320-326
1985
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394319
Hooper
Kinetics of reduction by subst ...
Nitrosomonas europaea
Eur. J. Biochem.
141
565-571
1984
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394327
Andersson
Mossbauer, EPR, and optical st ...
Nitrosomonas europaea
J. Biol. Chem.
259
6833-6840
1984
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394320
Hooper
Heme P460 of hydroxylamine oxi ...
Nitrosomonas europaea
Eur. J. Biochem.
134
83-87
1983
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394321
Lipscomb
Resolution of multiple heme ce ...
Nitrosomonas europaea
Biochemistry
21
3965-3972
1982
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394333
Hooper
Reaction of oxygen with hydrox ...
Nitrosomonas europaea, Nitrosomonas sp.
FEBS Lett.
144
299-303
1982
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394322
Terry
Hydroxylamine oxidoreductase: ...
Nitrosomonas europaea
Biochemistry
20
7026-7032
1981
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Yamanaka
-
Oxidation of hydroxylamine to ...
Nitrosomonas europaea
Curr. Microbiol.
4
239-244
1980
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394323
Hooper
Hydroxylamine oxidoreductase o ...
Nitrosomonas europaea, Nitrosomonas europaea Schmidt
Biochim. Biophys. Acta
571
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1979
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394324
Yamanaka
Highly purified hydroxylamine ...
Nitrosomonas europaea
J. Biochem.
86
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1979
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394325
Hooper
Hydroxylamine oxidoreductase f ...
Nitrosomonas europaea
Biochemistry
17
2984-2989
1978
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2
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394326
Hooper
Hydroxylamine oxidoreductase o ...
Nitrosomonas europaea
Biochim. Biophys. Acta
462
141-152
1977
1
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3
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3
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394330
Ritchie
The partial characterization o ...
Nitrosomonas europaea
Biochem. J.
138
471-480
1974
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6
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6
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394315
Rees
Studies of the hydroxylamine m ...
Nitrosomonas europaea
Biochemistry
7
353-366
1968
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394329
Rees
Studies on the hydroxylamine m ...
Nitrosomonas europaea
Biochemistry
7
366-372
1968
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