BRENDA - Enzyme Database
show all sequences of 1.9.6.1

Kinetics of substrate inhibition of periplasmic nitrate reductase

Jacques, J.G.; Burlat, B.; Arnoux, P.; Sabaty, M.; Guigliarelli, B.; Leger, C.; Pignol, D.; Fourmond, V.; Biochim. Biophys. Acta 1837, 1801-1809 (2014)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
nitrate
at high substrate concentration, substrate inhibition occurs, mechanism of substrate inhibition in Nap, and kinetics, overview
Rhodobacter sphaeroides
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics during activation and inactivation of the enzyme, chronoamperometry, overview. The inactive species exists under three redox states, and the active form must exist in different redox states within the catalytic cycle
Rhodobacter sphaeroides
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Rhodobacter sphaeroides
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Molybdenum
within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur
Rhodobacter sphaeroides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
Rhodobacter sphaeroides
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Rhodobacter sphaeroides DSM 158
-
2 ferricytochrome + nitrite
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
Q53176
-
-
Rhodobacter sphaeroides DSM 158
Q53176
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
-
741958
Rhodobacter sphaeroides
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
741958
Rhodobacter sphaeroides DSM 158
2 ferricytochrome + nitrite
-
-
-
?
additional information
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
741958
Rhodobacter sphaeroides
?
-
-
-
-
additional information
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
741958
Rhodobacter sphaeroides DSM 158
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterodimer
-
Rhodobacter sphaeroides
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Rhodobacter sphaeroides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
assay at
Rhodobacter sphaeroides
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c
two surface-exposed c-type hemes, NapB
Rhodobacter sphaeroides
molybdenum cofactor
i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview
Rhodobacter sphaeroides
[4Fe-4S] cluster
in close proximity to the MoCo
Rhodobacter sphaeroides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c
two surface-exposed c-type hemes, NapB
Rhodobacter sphaeroides
molybdenum cofactor
i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview
Rhodobacter sphaeroides
[4Fe-4S] cluster
in close proximity to the MoCo
Rhodobacter sphaeroides
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
nitrate
at high substrate concentration, substrate inhibition occurs, mechanism of substrate inhibition in Nap, and kinetics, overview
Rhodobacter sphaeroides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics during activation and inactivation of the enzyme, chronoamperometry, overview. The inactive species exists under three redox states, and the active form must exist in different redox states within the catalytic cycle
Rhodobacter sphaeroides
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Rhodobacter sphaeroides
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Molybdenum
within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur
Rhodobacter sphaeroides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
Rhodobacter sphaeroides
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Rhodobacter sphaeroides DSM 158
-
2 ferricytochrome + nitrite
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
-
741958
Rhodobacter sphaeroides
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
741958
Rhodobacter sphaeroides DSM 158
2 ferricytochrome + nitrite
-
-
-
?
additional information
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
741958
Rhodobacter sphaeroides
?
-
-
-
-
additional information
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
741958
Rhodobacter sphaeroides DSM 158
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
-
Rhodobacter sphaeroides
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Rhodobacter sphaeroides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
assay at
Rhodobacter sphaeroides
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the DMSO reductase family
Rhodobacter sphaeroides
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the DMSO reductase family
Rhodobacter sphaeroides
Other publictions for EC 1.9.6.1
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
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)
741478
Cerqueira
Periplasmic nitrate reductase ...
Desulfovibrio desulfuricans, Methylotenera mobilis, Methylotenera mobilis JLW8
Acc. Chem. Res.
48
2875-2884
2015
-
-
-
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1
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1
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2
3
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3
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3
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1
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-
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5
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1
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1
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3
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3
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1
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1
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2
3
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3
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-
-
5
-
1
-
-
-
1
-
-
-
-
5
5
-
-
-
742645
Lopez
The periplasmic nitrate reduc ...
Salmonella enterica, Salmonella enterica SL1344 AND CAL128
Infect. Immun.
83
3470-3478
2015
-
-
1
-
1
-
-
-
1
-
-
2
-
6
-
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2
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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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-
2
-
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-
-
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-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
741958
Jacques
Kinetics of substrate inhibit ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides DSM 158
Biochim. Biophys. Acta
1837
1801-1809
2014
-
-
-
-
-
-
1
1
1
1
-
2
-
2
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4
1
1
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1
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3
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3
-
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1
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1
1
1
-
2
-
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-
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4
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
742380
Sanchez
The nitrate-sensing NasST sys ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum JCM 10833
Environ. Microbiol.
16
3263-3274
2014
-
-
1
-
1
-
-
-
1
-
-
-
-
5
-
-
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-
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
2
3
3
2
-
-
742486
Dow
Characterization of a peripla ...
Escherichia coli
FEBS J.
281
246-260
2014
1
-
1
1
1
-
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1
2
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1
-
4
-
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1
-
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1
1
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3
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1
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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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-
-
-
-
-
-
2
2
-
-
-
742319
Gonzalez
-
Periplasmic nitrate reductase ...
Anaeromyxobacter dehalogenans, Bradyrhizobium japonicum, Campylobacter jejuni subsp. jejuni, Campylobacter jejuni subsp. jejuni ATCC 700819, Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1, Desulfitobacterium hafniense, Desulfovibrio desulfuricans, Escherichia coli, Paracoccus denitrificans, Paracoccus pantotrophus, Paracoccus pantotrophus GB17, Pseudomonas sp., Pseudomonas sp. G-179, Rhodobacter sphaeroides, Shewanella gelidimarina, Shewanella oneidensis, Wolinella succinogenes
Coord. Chem. Rev.
257
315-331
2013
-
-
14
-
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-
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14
28
-
18
-
18
-
-
-
14
-
-
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-
18
14
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-
-
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-
42
-
-
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-
14
42
-
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-
14
28
-
18
-
-
-
-
-
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-
18
14
-
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-
-
-
-
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25
25
-
-
-
742648
Cerqueira
The sulfur shift an activatio ...
Desulfovibrio desulfuricans
Inorg. Chem.
52
10766-10772
2013
-
-
-
1
-
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-
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1
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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2
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2
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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712967
Simpson
The periplasmic nitrate reduct ...
Shewanella amazonensis, Shewanella amazonensis SB2B, Shewanella baltica, Shewanella baltica OS155, Shewanella baltica OS185, Shewanella baltica OS195, Shewanella baltica OS223, Shewanella denitrificans, Shewanella denitrificans OS217, Shewanella frigidimarina, Shewanella halifaxensis, Shewanella loihica, Shewanella loihica PV-4, Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550, Shewanella pealeana, Shewanella piezotolerans, Shewanella piezotolerans WP3, Shewanella putrefaciens, Shewanella putrefaciens CN-32, Shewanella sediminis, Shewanella sp., Shewanella sp. ANA-3, Shewanella sp. MR-4, Shewanella sp. MR-7, Shewanella sp. W3-18-1, Shewanella woodyi
Microbiology
156
302-312
2010
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42
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27
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26
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26
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27
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696917
Durvasula
Effect of periplasmic nitrate ...
Paracoccus pantotrophus
Biotechnol. Prog.
25
973-979
2009
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1
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1
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1
1
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698636
Stewart
Catabolite repression control ...
Paracoccus pantotrophus
J. Bacteriol.
191
996-1005
2009
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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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699015
Hofmann
Density functional theory stud ...
Desulfovibrio desulfuricans
J. Biol. Inorg. Chem.
14
1023-1035
2009
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1
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1
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699199
Cerqueira
The effect of the sixth sulfur ...
Desulfovibrio desulfuricans
J. Comput. Chem.
30
2466-2484
2009
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1
1
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711653
Van Alst
Compensatory periplasmic nitra ...
Pseudomonas aeruginosa
Can. J. Microbiol.
55
1133-1144
2009
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1
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2
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1
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1
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684990
Gates
Voltammetric characterization ...
Paracoccus pantotrophus
Biochem. J.
409
159-168
2008
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2
1
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695337
Coelho
Heterodimeric nitrate reductas ...
Cupriavidus necator H16
Acta Crystallogr. Sect. F
63
516-519
2007
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1
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674891
Jepson
Spectropotentiometric and stru ...
Escherichia coli
J. Biol. Chem.
282
6425-6437
2006
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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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2
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1
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1
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675847
Nilavongse
The NapF protein of the Escher ...
Escherichia coli
Microbiology
152
3227-3237
2006
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