BRENDA - Enzyme Database
show all sequences of 1.7.2.6

Epsilonproteobacterial hydroxylamine oxidoreductase (epsilonHao) characterization of a missing link in the multihaem cytochrome c family

Haase, D.; Hermann, B.; Einsle, O.; Simon, J.; Mol. Microbiol. 105, 127-138 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Wolinella succinogenes as maltose binding protein fusion
Campylobacter fetus
expression in Wolinella succinogenes as maltose binding protein fusion
Caminibacter mediatlanticus
expression in Wolinella succinogenes as maltose binding protein fusion
Nautilia profundicola
expression in Wolinella succinogenes as maltose binding protein fusion
Campylobacter curvus
Engineering
Protein Variants
Commentary
Organism
W428Y
mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity decreases considerably
Campylobacter curvus
W434Y
mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity decreases considerably
Campylobacter fetus
W464Y
mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity increases 3fold
Caminibacter mediatlanticus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.89
-
nitrite
wild-type, pH 7.0, 37°C
Campylobacter fetus
1.5
-
nitrite
wild-type, pH 7.0, 37°C
Caminibacter mediatlanticus
1.9
-
hydroxylamine
wild-type, pH 7.0, 37°C
Campylobacter fetus
2.39
-
nitrite
mutant W434Y, pH 7.0, 37°C
Campylobacter fetus
2.7
-
nitrite
wild-type, pH 7.0, 37°C
Campylobacter curvus
2.99
-
nitrite
mutant W428Y, pH 7.0, 37°C
Campylobacter curvus
4.6
-
nitrite
mutant W464Y, pH 7.0, 37°C
Caminibacter mediatlanticus
6
-
hydroxylamine
wild-type, pH 7.0, 37°C
Caminibacter mediatlanticus
6.6
-
hydroxylamine
wild-type, pH 7.0, 37°C
Campylobacter curvus
6.75
-
hydroxylamine
mutant W428Y, pH 7.0, 37°C
Campylobacter curvus
7.4
-
hydroxylamine
mutant W434Y, pH 7.0, 37°C
Campylobacter fetus
16.9
-
hydroxylamine
mutant W464Y, pH 7.0, 37°C
Caminibacter mediatlanticus
Organism
Organism
UniProt
Commentary
Textmining
Caminibacter mediatlanticus
-
-
-
Campylobacter curvus
-
-
-
Campylobacter fetus
-
-
-
Nautilia profundicola
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1
-
nitrite reduction, pH 7.0, 37°C
Caminibacter mediatlanticus
1.2
-
nitrite reduction, pH 7.0, 37°C
Nautilia profundicola
27
-
nitrite reduction, pH 7.0, 37°C
Campylobacter curvus
29
-
hydroxylamine reduction, pH 7.0, 37°C
Nautilia profundicola
68
-
hydroxylamine reduction, pH 7.0, 37°C
Campylobacter curvus
149
-
hydroxylamine reduction, pH 7.0, 37°C
Campylobacter fetus
158
-
hydroxylamine reduction, pH 7.0, 37°C
Caminibacter mediatlanticus
181
-
nitrite reduction, pH 7.0, 37°C
Campylobacter fetus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Campylobacter fetus
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Caminibacter mediatlanticus
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Nautilia profundicola
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Campylobacter curvus
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Campylobacter fetus
NH3 + oxidized phenazine methosulfate
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Caminibacter mediatlanticus
NH3 + oxidized phenazine methosulfate
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Nautilia profundicola
NH3 + oxidized phenazine methosulfate
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Campylobacter curvus
NH3 + oxidized phenazine methosulfate
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Campylobacter fetus
?
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Caminibacter mediatlanticus
?
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Nautilia profundicola
?
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Campylobacter curvus
?
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Campylobacter fetus
NH4+ + reduced methyl viologen + H2O
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Caminibacter mediatlanticus
NH4+ + reduced methyl viologen + H2O
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Nautilia profundicola
NH4+ + reduced methyl viologen + H2O
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Campylobacter curvus
NH4+ + reduced methyl viologen + H2O
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
haoA
-
Campylobacter fetus
haoA
-
Caminibacter mediatlanticus
haoA
-
Nautilia profundicola
haoA
-
Campylobacter curvus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Wolinella succinogenes as maltose binding protein fusion
Campylobacter fetus
expression in Wolinella succinogenes as maltose binding protein fusion
Caminibacter mediatlanticus
expression in Wolinella succinogenes as maltose binding protein fusion
Nautilia profundicola
expression in Wolinella succinogenes as maltose binding protein fusion
Campylobacter curvus
Engineering (protein specific)
Protein Variants
Commentary
Organism
W428Y
mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity decreases considerably
Campylobacter curvus
W434Y
mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity decreases considerably
Campylobacter fetus
W464Y
mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity increases 3fold
Caminibacter mediatlanticus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.89
-
nitrite
wild-type, pH 7.0, 37°C
Campylobacter fetus
1.5
-
nitrite
wild-type, pH 7.0, 37°C
Caminibacter mediatlanticus
1.9
-
hydroxylamine
wild-type, pH 7.0, 37°C
Campylobacter fetus
2.39
-
nitrite
mutant W434Y, pH 7.0, 37°C
Campylobacter fetus
2.7
-
nitrite
wild-type, pH 7.0, 37°C
Campylobacter curvus
2.99
-
nitrite
mutant W428Y, pH 7.0, 37°C
Campylobacter curvus
4.6
-
nitrite
mutant W464Y, pH 7.0, 37°C
Caminibacter mediatlanticus
6
-
hydroxylamine
wild-type, pH 7.0, 37°C
Caminibacter mediatlanticus
6.6
-
hydroxylamine
wild-type, pH 7.0, 37°C
Campylobacter curvus
6.75
-
hydroxylamine
mutant W428Y, pH 7.0, 37°C
Campylobacter curvus
7.4
-
hydroxylamine
mutant W434Y, pH 7.0, 37°C
Campylobacter fetus
16.9
-
hydroxylamine
mutant W464Y, pH 7.0, 37°C
Caminibacter mediatlanticus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1
-
nitrite reduction, pH 7.0, 37°C
Caminibacter mediatlanticus
1.2
-
nitrite reduction, pH 7.0, 37°C
Nautilia profundicola
27
-
nitrite reduction, pH 7.0, 37°C
Campylobacter curvus
29
-
hydroxylamine reduction, pH 7.0, 37°C
Nautilia profundicola
68
-
hydroxylamine reduction, pH 7.0, 37°C
Campylobacter curvus
149
-
hydroxylamine reduction, pH 7.0, 37°C
Campylobacter fetus
158
-
hydroxylamine reduction, pH 7.0, 37°C
Caminibacter mediatlanticus
181
-
nitrite reduction, pH 7.0, 37°C
Campylobacter fetus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Campylobacter fetus
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Caminibacter mediatlanticus
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Nautilia profundicola
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
743303
Campylobacter curvus
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Campylobacter fetus
NH3 + oxidized phenazine methosulfate
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Caminibacter mediatlanticus
NH3 + oxidized phenazine methosulfate
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Nautilia profundicola
NH3 + oxidized phenazine methosulfate
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
-
743303
Campylobacter curvus
NH3 + oxidized phenazine methosulfate
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Campylobacter fetus
?
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Caminibacter mediatlanticus
?
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Nautilia profundicola
?
-
-
-
?
additional information
hydroxylamine oxidation is negligible
743303
Campylobacter curvus
?
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Campylobacter fetus
NH4+ + reduced methyl viologen + H2O
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Caminibacter mediatlanticus
NH4+ + reduced methyl viologen + H2O
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Nautilia profundicola
NH4+ + reduced methyl viologen + H2O
-
-
-
?
nitrite + reduced benzyl viologen + H+
-
743303
Campylobacter curvus
NH4+ + reduced methyl viologen + H2O
-
-
-
?
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
-
-
-
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
-
-
-
-
-
-
-
-
11
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
11
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
724393
Cedervall
Structural studies of hydroxyl ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Biochemistry
52
6211-6218
2013
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725301
Keluskar
Evaluation of hydroxylamine ox ...
Nitrosomonas europaea
J. Basic Microbiol.
54
261-268
2013
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
711263
Kostera
Enzymatic interconversion of a ...
Nitrosomonas europaea
Biochemistry
49
8546-8553
2010
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725885
Hozuki
Effect of salinity on hydroxyl ...
Nitrosococcus oceani, Nitrosococcus oceani NS58
Microbes Environ.
25
95-102
2010
-
-
-
-
-
-
-
2
-
-
1
-
-
2
-
-
1
-
-
-
-
-
4
2
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
1
-
-
-
-
1
-
-
-
-
4
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
696882
Radniecki
Expression of merA, trxA, amoA ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Biotechnol. Bioeng.
104
1004-1011
2009
-
-
-
-
-
-
2
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710728
Cedervall
Crystallization and preliminar ...
Nitrosomonas europaea
Acta Crystallogr. Sect. F
65
1296-1298
2009
-
-
-
2
-
-
-
-
-
-
1
1
-
1
-
-
2
-
-
-
-
-
1
2
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
1
1
-
-
-
2
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674203
Pulcu
Direct electrochemistry of tet ...
Nitrosomonas europaea
J. Am. Chem. Soc.
129
1838-1839
2007
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
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Transcriptional analysis of th ...
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658903
Cabail
Laser photoinitiated nitrosyla ...
Nitrosomonas europaea
Inorg. Chem.
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2005
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Kurnikov
Redox equilibria in hydroxylam ...
Nitrosomonas europaea
Biochemistry
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656327
Tokuyama
Nitrosomonas communis strain Y ...
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J. Biosci. Bioeng.
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658900
Cabail
Selective one-electron reducti ...
Nitrosomonas europaea
Inorg. Chem.
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2003
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657688
Arp
Molecular biology and biochemi ...
Nitrosomonas europaea
Arch. Microbiol.
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657690
Hommes
The roles of the three gene co ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Arch. Microbiol.
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2002
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657930
Hendrich
Spectroscopic characterization ...
Nitrosomonas europaea
Biochemistry
41
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2002
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394338
Hendrich
Correlations of structure and ...
Nitrosomonas europaea
J. Am. Chem. Soc.
123
2997-3005
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394346
Yamagata
Mutational analysis of the mul ...
Nitrosomonas europaea, Nitrosomonas sp., Nitrosomonas sp. ENI-11, Nitrosomonas europaea ENI-11
Biosci. Biotechnol. Biochem.
64
1754-1757
2000
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394335
Arciero
Correlation of optical and EPR ...
Nitrosomonas europaea
Biochemistry
37
523-529
1998
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394343
Nejidat
Effect of ammonia starvation o ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
J. Biochem.
121
957-960
1997
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720525
Igarashi
The 2.8 A structure of hydroxy ...
Nitrosomonas europaea
Nat. Struct. Biol.
4
276-284
1997
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Hommes
Mutagenesis of hydroxylamine o ...
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19178
J. Bacteriol.
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1996
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394341
Logan
Suicide Inactivation of Hydrox ...
Nitrosomonas europaea
Biochemistry
34
9257-9264
1995
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639387
Logan
Reaction with cyanide of hydro ...
Nitrosomonas europaea
Biochemistry
34
9028-9037
1995
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Zahn
Oxidation of hydroxylamine by ...
Methylococcus capsulatus
J. Bacteriol.
176
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1994
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719635
Hendrich
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The active site of hydroxylami ...
Nitrosomonas europaea, Nitrosomonas europaea Schmidt
J. Am. Chem. Soc.
116
11961-11968
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Arciero
Hydroxylamine oxidoreductase f ...
Nitrosomonas europaea
J. Biol. Chem.
268
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1993
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Collins
Optical spectropotentiometric ...
Nitrosomonas europaea
J. Biol. Chem.
268
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1993
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718820
Hooper
Spectroscopic and rapid kineti ...
Nitrosomonas europaea
Biochemistry
30
11466-11472
1991
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394332
Numata
Cytochrome p-460 of Nitrosomon ...
Nitrosomonas europaea
J. Biochem.
108
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1990
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394316
Tatsuaki
-
Cloning and expression of the ...
Nitrosomonas europaea
Hakko Kogaku Kaishi
66
103-107
1988
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394317
Balny
Effect of solvent, pressure an ...
Nitrosomonas europaea
Eur. J. Biochem.
176
273-279
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
J. Am. Chem. Soc.
109
2549-2550
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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Andersson
Mossbauer, EPR, and optical st ...
Nitrosomonas europaea
J. Biol. Chem.
259
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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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1
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1
1
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1
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1
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1
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1
1
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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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1
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2
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1
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394322
Terry
Hydroxylamine oxidoreductase: ...
Nitrosomonas europaea
Biochemistry
20
7026-7032
1981
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3
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1
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1
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1
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3
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1
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394334
Yamanaka
-
Oxidation of hydroxylamine to ...
Nitrosomonas europaea
Curr. Microbiol.
4
239-244
1980
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1
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4
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1
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1
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1
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4
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394323
Hooper
Hydroxylamine oxidoreductase o ...
Nitrosomonas europaea, Nitrosomonas europaea Schmidt
Biochim. Biophys. Acta
571
12-20
1979
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4
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3
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3
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1
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4
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2
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5
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3
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1
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4
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394324
Yamanaka
Highly purified hydroxylamine ...
Nitrosomonas europaea
J. Biochem.
86
1101-1108
1979
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1
5
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1
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1
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1
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1
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1
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5
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1
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1
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1
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394325
Hooper
Hydroxylamine oxidoreductase f ...
Nitrosomonas europaea
Biochemistry
17
2984-2989
1978
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1
1
1
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1
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1
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1
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2
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1
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1
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1
1
1
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1
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1
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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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1
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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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1
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1
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1
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1
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3
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2
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2
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1
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1
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1
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1
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1
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3
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2
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394329
Rees
Studies on the hydroxylamine m ...
Nitrosomonas europaea
Biochemistry
7
366-372
1968
-
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1
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1
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1
1
1
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2
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2
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1
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1
1
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