BRENDA - Enzyme Database
show all sequences of 1.7.2.4

The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity

Fernandes, A.T.; Damas, J.M.; Todorovic, S.; Huber, R.; Baratto, M.C.; Pogni, R.; Soares, C.M.; Martins, L.O.; FEBS J. 277, 3176-3189 (2010)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Pyrobaculum aerophilum
Crystallization (Commentary)
Crystallization (Commentary)
Organism
modeling of structure. The residues contributing to the semiocclusion of the T1 copper site are Trp355, Met389, and Met297. There is a negatively charged residue in the neighborhood of the T1 site, Glu296
Pyrobaculum aerophilum
Engineering
Protein Variants
Commentary
Organism
E296Q
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
M297A
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
M389A
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
W355A
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.032
-
N2O
pH 7.6, 25°C
Pyrobaculum aerophilum
0.033
-
Fe2+
pH 7.6, 25°C
Pyrobaculum aerophilum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
copper
3.2 mol of copper per mol of enzyme, in the as-isolated form. Presence of 0.1 mM enhances enzymic activity by 2fold
Pyrobaculum aerophilum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49600
-
gel fitlration
Pyrobaculum aerophilum
52000
-
1 * 52900, calculated, 1 * 52000, SDS-PAGE
Pyrobaculum aerophilum
52900
-
1 * 52900, calculated, 1 * 52000, SDS-PAGE
Pyrobaculum aerophilum
Organism
Organism
UniProt
Commentary
Textmining
Pyrobaculum aerophilum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
enzyme shows Cu+/Fe2+ oxidation kinetics that follow the Michaelis-Menten model, with 2fold to 10fold higher efficiencies for Cu+ and Fe2+ as compared with the tested aromatic compounds
724958
Pyrobaculum aerophilum
?
-
-
-
-
N2O + 2 Fe2+ + 2 H+
-
724958
Pyrobaculum aerophilum
N2 + H2O + 2 Fe3+
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 52900, calculated, 1 * 52000, SDS-PAGE
Pyrobaculum aerophilum
Synonyms
Synonyms
Commentary
Organism
McoP
-
Pyrobaculum aerophilum
multicopper oxidase
-
Pyrobaculum aerophilum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
85
-
-
Pyrobaculum aerophilum
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
85
-
half-life 5.5 h
Pyrobaculum aerophilum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
8
-
N2O
pH 7.6, 25°C
Pyrobaculum aerophilum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pyrobaculum aerophilum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
modeling of structure. The residues contributing to the semiocclusion of the T1 copper site are Trp355, Met389, and Met297. There is a negatively charged residue in the neighborhood of the T1 site, Glu296
Pyrobaculum aerophilum
Engineering (protein specific)
Protein Variants
Commentary
Organism
E296Q
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
M297A
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
M389A
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
W355A
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
Pyrobaculum aerophilum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.032
-
N2O
pH 7.6, 25°C
Pyrobaculum aerophilum
0.033
-
Fe2+
pH 7.6, 25°C
Pyrobaculum aerophilum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
copper
3.2 mol of copper per mol of enzyme, in the as-isolated form. Presence of 0.1 mM enhances enzymic activity by 2fold
Pyrobaculum aerophilum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49600
-
gel fitlration
Pyrobaculum aerophilum
52000
-
1 * 52900, calculated, 1 * 52000, SDS-PAGE
Pyrobaculum aerophilum
52900
-
1 * 52900, calculated, 1 * 52000, SDS-PAGE
Pyrobaculum aerophilum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
enzyme shows Cu+/Fe2+ oxidation kinetics that follow the Michaelis-Menten model, with 2fold to 10fold higher efficiencies for Cu+ and Fe2+ as compared with the tested aromatic compounds
724958
Pyrobaculum aerophilum
?
-
-
-
-
N2O + 2 Fe2+ + 2 H+
-
724958
Pyrobaculum aerophilum
N2 + H2O + 2 Fe3+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 52900, calculated, 1 * 52000, SDS-PAGE
Pyrobaculum aerophilum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
85
-
-
Pyrobaculum aerophilum
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
85
-
half-life 5.5 h
Pyrobaculum aerophilum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
8
-
N2O
pH 7.6, 25°C
Pyrobaculum aerophilum
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
242
-
Fe2+
pH 7.6, 25°C
Pyrobaculum aerophilum
250
-
N2O
pH 7.6, 25°C
Pyrobaculum aerophilum
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
242
-
Fe2+
pH 7.6, 25°C
Pyrobaculum aerophilum
250
-
N2O
pH 7.6, 25°C
Pyrobaculum aerophilum
Other publictions for EC 1.7.2.4
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)
742390
Sanchez
Regulation of nitrous oxide r ...
Bradyrhizobium diazoefficiens
Environ. Microbiol. Rep.
9
389-396
2017
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-
1
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2
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1
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3
2
2
3
-
-
742753
Johnston
Spectroscopic definition of t ...
Marinobacter hydrocarbonoclasticus, Marinobacter hydrocarbonoclasticus 617
J. Am. Chem. Soc.
139
4462-4476
2017
-
-
-
-
-
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1
-
1
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2
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3
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1
1
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1
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4
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3
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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1
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1
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1
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4
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1
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1
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-
741924
Schneider
Role of calcium in secondary ...
Shewanella denitrificans, Shewanella denitrificans OS217
Biochemistry
55
1433-1440
2016
-
-
1
1
-
-
-
-
1
2
1
2
-
4
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1
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4
2
6
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1
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1
1
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1
2
1
2
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1
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4
2
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2
2
-
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-
742384
Qu
Transcriptional and metabolic ...
Paracoccus denitrificans
Environ. Microbiol.
18
2951-2963
2016
-
-
1
-
-
-
1
-
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1
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1
-
3
1
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1
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2
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3
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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
-
-
2
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
741746
Zhang
Response of denitrifying gene ...
uncultured bacterium
Appl. Microbiol. Biotechnol.
99
4059-4070
2015
-
-
1
-
-
-
-
-
-
-
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1
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-
-
-
-
-
-
-
1
1
1
1
-
-
742272
Johnston
Protonation state of the Cu4S ...
Paracoccus pantotrophus, Pseudomonas stutzeri
Chem. Sci.
6
5670-5679
2015
-
-
-
-
-
-
-
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2
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3
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-
-
-
741677
Wyman
Denitrifying alphaproteobacte ...
alpha proteobacterium 4N, Trichodesmium erythraeum, Trichodesmium erythraeum IMS01, uncultured Alphaproteobacteria bacterium
Appl. Environ. Microbiol.
79
2670-2681
2013
-
-
3
-
-
-
-
-
-
-
-
4
-
8
-
-
-
-
-
-
-
-
4
-
9
-
-
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3
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3
3
-
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4
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-
-
-
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-
-
4
-
-
-
-
-
-
-
-
-
-
6
6
-
-
-
725551
Ertem
N-O bond cleavage mechanism(s) ...
Paracoccus denitrificans
J. Biol. Inorg. Chem.
17
687-698
2012
-
-
-
1
-
-
-
-
-
-
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2
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1
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1
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-
-
-
725648
Fujita
Direct electron transfer from ...
Achromobacter cycloclastes
J. Inorg. Biochem.
115
163-173
2012
-
-
-
-
-
-
-
3
-
-
-
1
-
4
-
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2
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1
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2
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3
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1
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-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
726100
DellAcqua
Biochemical characterization o ...
Marinobacter hydrocarbonoclasticus
Philos. Trans. R. Soc. Lond. B Biol. Sci.
367
1204-1212
2012
-
-
-
-
-
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2
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1
1
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4
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2
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1
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1
1
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4
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2
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-
-
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-
-
-
726523
Wan
Expression of the nos operon p ...
Pseudomonas stutzeri, Pseudomonas stutzeri ATCC 14405
Transgenic Res.
21
593-603
2012
-
1
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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1
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2
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-
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-
724958
Fernandes
The multicopper oxidase from t ...
Pyrobaculum aerophilum
FEBS J.
277
3176-3189
2010
-
-
1
1
4
-
-
2
-
1
3
-
-
5
-
-
-
-
-
-
-
-
2
1
2
1
-
1
1
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1
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1
4
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2
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1
3
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-
2
1
1
-
1
1
-
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-
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-
-
2
2
700984
Savelieff
Experimental evidence for a li ...
Paracoccus denitrificans
Proc. Natl. Acad. Sci. USA
105
7919-7924
2008
-
-
1
-
-
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1
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3
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1
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1
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-
698268
Fujita
Insights into the mechanism of ...
Achromobacter cycloclastes
Inorg. Chem.
46
613-615
2007
-
-
-
-
-
-
-
1
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1
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1
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2
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2
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1
1
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1
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2
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1
1
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698456
Ghosh
Spectroscopic, computational, ...
Achromobacter cycloclastes, Marinobacter hydrocarbonoclasticus
J. Am. Chem. Soc.
129
3955-3965
2007
-
-
-
-
-
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2
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5
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6
2
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2
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-
699384
Fujita
Anaerobic purification, charac ...
Achromobacter cycloclastes, Achromobacter cycloclastes IAM1013
J. Inorg. Biochem.
101
1836-1844
2007
-
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1
-
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1
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1
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2
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3
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1
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1
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2
1
2
1
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1
1
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1
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-
-
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-
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1
-
1
-
2
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1
-
-
1
-
2
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
700303
Bingham
-
Magnetic circular dichroism an ...
Paracoccus pantotrophus
Mol. Phys.
105
2169-2176
2007
-
-
-
-
-
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1
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1
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-
-
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1
1
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-
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1
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1
-
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-
-
-
671444
Horn
Nitrous oxide reductase genes ...
Dechloromonas denitrificans, Flavobacterium denitrificans, Pseudomonas sp., Pseudomonas sp. ED3
Appl. Environ. Microbiol.
72
1019-1026
2006
-
-
-
-
-
-
-
-
-
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-
13
-
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-
1
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4
-
3
-
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671455
Sameshima-Saito
Symbiotic Bradyrhizobium japon ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
Appl. Environ. Microbiol.
72
2526-2532
2006
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24
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2
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671469
Henry
Quantitative detection of the ...
Achromobacter cycloclastes, Alcaligenes faecalis, Bradyrhizobium japonicum, Ensifer adhaerens, Ensifer adhaerens SN611, Hyphomicrobium denitrificans, Pseudomonas denitrificans (nomen rejiciendum), Pseudomonas denitrificans (nomen rejiciendum) CCUG 2519, Pseudomonas fluorescens, Pseudomonas fluorescens C7R12, Sinorhizobium meliloti, Sinorhizobium meliloti 50
Appl. Environ. Microbiol.
72
5181-5189
2006
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12
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672074
Taubner
Structural studies of Apo NosL ...
Achromobacter cycloclastes
Biochemistry
45
12240-12252
2006
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1
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674195
Gorelsky
Mechanism of N2O reduction by ...
Pseudomonas sp.
J. Am. Chem. Soc.
128
278-290
2006
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675403
Paraskevopoulos
Insight into catalysis of nitr ...
Achromobacter cycloclastes 1013, Achromobacter cycloclastes
J. Mol. Biol.
362
55-65
2006
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1
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660478
Mattila
How does nitrous oxide reducta ...
Paracoccus denitrificans, Rhodobacter sphaeroides
Proteins
59
708-722
2005
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2
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4
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5
1
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673234
Rasmussen
Formation of a cytochrome c-ni ...
Paracoccus pantotrophus
Dalton Trans.
2005
3501-3506
2005
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1
1
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4
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673622
Wunsch
NosX function connects to nitr ...
Paracoccus denitrificans
FEBS Lett.
579
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2005
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657567
Velasco
Molecular characterization of ...
Bradyrhizobium japonicum
Antonie van Leeuwenhoek
85
229-235
2004
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658979
Chan
Reductively activated nitrous ...
Achromobacter cycloclastes
J. Am. Chem. Soc.
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2004
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394516
Haltia
The crystal structure of nitro ...
Paracoccus denitrificans
Biochem. J.
369
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2003
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1
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Yamaguchi
Characterization of nitrous ox ...
Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151
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2003
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1
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2
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4
1
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1
1
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659880
Arai
Transcriptional regulation of ...
Pseudomonas aeruginosa
Microbiology
149
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2003
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1
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1
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1
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394517
Rasmussen
Multiple forms of the catalyti ...
Paracoccus pantotrophus
Biochem. J.
364
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2002
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5
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2
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394518
Rasmussen
The catalytic center in nitrou ...
Paracoccus pantotrophus, Pseudomonas stutzeri
Biochemistry
39
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2000
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2
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1
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2
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394519
Prudencio
Purification, Characterization ...
Marinobacter hydrocarbonoclasticus, Marinobacter hydrocarbonoclasticus 617
Biochemistry
39
3899-3907
2000
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1
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3
2
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6
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1
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2
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2
1
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394520
Brown
A novel type of catalytic copp ...
Marinobacter hydrocarbonoclasticus, Marinobacter hydrocarbonoclasticus 617
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7
191-195
2000
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1
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1
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1
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394521
Sato
Anaerobic purification and cha ...
Rhodobacter sphaeroides
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1999
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1
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2
1
2
1
1
-
1
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1
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394522
Sabaty
Nitrite and nitrous oxide redu ...
Rhodobacter sphaeroides
J. Bacteriol.
181
6028-6032
1999
1
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1
-
-
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-
-
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-
-
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394523
Ferretti
Biochemical characterization a ...
Achromobacter xylosoxidans
Eur. J. Biochem.
259
651-659
1999
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1
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2
1
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1
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1
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394524
Sato
Characterization of a multi-co ...
Rhodobacter sphaeroides
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3
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1
3
1
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1
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1
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2
1
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-
-
-
-
-
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394525
Farrar
CuA and CuZ are variants of th ...
Pseudomonas stutzeri
Proc. Natl. Acad. Sci. USA
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1998
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1
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1
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1
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-
-
-
-
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394526
Hole
Characterization of the membra ...
Thiobacillus denitrificans
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1
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1
2
1
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1
-
1
1
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-
-
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394527
Dreusch
Mutation of the conserved Cys1 ...
Pseudomonas stutzeri
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1
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1
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1
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1
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394528
Zhang
-
The reaction of reduced cytoch ...
Wolinella succinogenes
Biochim. Biophys. Acta
1142
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1993
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1
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2
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Berks
Purification and characterizat ...
Paracoccus pantotrophus, Paracoccus pantotrophus LMD 82.5
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4
1
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3
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SooHoo
Purification and characterizat ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa P2
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2
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2
1
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394530
Jones
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Denitrification in Flexibacter ...
Solitalea canadensis
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36
430-434
1990
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1
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394531
Hulse
Isolation of a high specific a ...
Achromobacter cycloclastes
Biochem. Biophys. Res. Commun.
166
729-735
1990
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1
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2
1
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1
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1
1
1
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2
1
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Bonin
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Effects of oxygen on each step ...
Marinobacter hydrocarbonoclasticus
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1989
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394533
Teraguchi
Purification and some characte ...
Wolinella succinogenes
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Viebrock
Molecular cloning, heterologou ...
Pseudomonas stutzeri
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1988
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394535
Coyne
Nitrous oxide reduction in nod ...
Rhizobium sp., Rhizobium sp. 8A55
Appl. Environ. Microbiol.
53
1168-1170
1987
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394536
Snyder
Purification and some characte ...
Paracoccus denitrificans
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262
6515-6525
1987
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394538
Michalski
-
Purification and characterizat ...
Rhodobacter sphaeroides
Biochim. Biophys. Acta
872
50-60
1986
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394542
Aida
Temporary low oxygen condition ...
Pseudomonas sp., Pseudomonas sp. G59
Can. J. Microbiol.
32
543-547
1986
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394539
Coyle
Nitrous oxide reductase from d ...
Pseudomonas stutzeri
Eur. J. Biochem.
153
459-467
1985
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394540
McEwan
Nitrous oxide reduction by mem ...
Rhodobacter capsulatus, Rhodobacter sphaeroides, Rhodopseudomonas palustris, Rhodopseudomonas palustris PW5, Rhodospirillum rubrum, Rhodospirillum rubrum S1
J. Bacteriol.
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823-830
1985
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6
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394537
Kucera
-
Amperometric assay of activity ...
Paracoccus denitrificans
Collect. Czech. Chem. Commun.
49
2709-2712
1984
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394541
Snyder
Nitrous oxide reductase and th ...
Paracoccus denitrificans, Pseudomonas denitrificans (nomen rejiciendum), Pseudomonas stutzeri
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588-592
1984
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6
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394543
Zumft
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A novel kind of multi-copper p ...
Pseudomonas stutzeri
FEBS Lett.
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107-112
1982
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Matsubara
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Identification of a copper pro ...
Pseudomonas fluorescens
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322-328
1982
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394545
Kristjansson
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Partial purification and chara ...
Paracoccus denitrificans
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247-251
1981
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Kristjansson
First practical assay for solu ...
Paracoccus denitrificans
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704-707
1980
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