BRENDA - Enzyme Database show
show all sequences of 1.15.1.2

Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site

Bonnot, F.; Duval, S.; Lombard, M.; Valton, J.; Houee-Levin, C.; Niviere, V.; J. Biol. Inorg. Chem. 16, 889-898 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant SORs, and of rubredoxin in Escherichia coli strain BL21(DE3)
Desulfarculus baarsii
Engineering
Amino acid exchange
Commentary
Organism
C13S
site-directed mutagenesis, the lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide
Desulfarculus baarsii
Y115A
site-directed mutagenesis, the Y115A SOR mutant folds properly, this mutation does not affect the general properties of the two iron sites of SOR
Desulfarculus baarsii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow kinetic analysis, overview
Desulfarculus baarsii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
2Fe-SOR contains iron center I and iron center II, function of iron center I as an electronic relay between a reductase enzyme and iron center II, overview. The active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, which functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction
Desulfarculus baarsii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Desulfarculus baarsii
in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview
?
-
-
-
reduced rubredoxin + superoxide + 2 H+
Desulfarculus baarsii
-
rubredoxin + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Desulfarculus baarsii
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant SORs, and rubredoxin from Escherichia coli strain BL21(DE3) to homogeneity by anion exchange chromatography and gel filtration
Desulfarculus baarsii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview
715670
Desulfarculus baarsii
?
-
-
-
-
additional information
artificial reduction of the SOR iron active site using the NADPH:flavodoxin oxidoreductase from Escherichia coli
715670
Desulfarculus baarsii
?
-
-
-
-
reduced rubredoxin + superoxide + 2 H+
-
715670
Desulfarculus baarsii
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
the mononuclear iron center with an FeN4S1 coordination catalyzes the one electron reduction of superoxide to form hydrogen peroxide in presence of an additional rubredoxin-like desulforedoxin iron center
715670
Desulfarculus baarsii
rubredoxin + H2O2
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
three-dimensional structure of the homodimeric SOR, modelling, overview
Desulfarculus baarsii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Desulfarculus baarsii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Desulfarculus baarsii
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, that functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction
Desulfarculus baarsii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant SORs, and of rubredoxin in Escherichia coli strain BL21(DE3)
Desulfarculus baarsii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, that functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction
Desulfarculus baarsii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C13S
site-directed mutagenesis, the lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide
Desulfarculus baarsii
Y115A
site-directed mutagenesis, the Y115A SOR mutant folds properly, this mutation does not affect the general properties of the two iron sites of SOR
Desulfarculus baarsii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow kinetic analysis, overview
Desulfarculus baarsii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
2Fe-SOR contains iron center I and iron center II, function of iron center I as an electronic relay between a reductase enzyme and iron center II, overview. The active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, which functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction
Desulfarculus baarsii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Desulfarculus baarsii
in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview
?
-
-
-
reduced rubredoxin + superoxide + 2 H+
Desulfarculus baarsii
-
rubredoxin + H2O2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant SORs, and rubredoxin from Escherichia coli strain BL21(DE3) to homogeneity by anion exchange chromatography and gel filtration
Desulfarculus baarsii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview
715670
Desulfarculus baarsii
?
-
-
-
-
additional information
artificial reduction of the SOR iron active site using the NADPH:flavodoxin oxidoreductase from Escherichia coli
715670
Desulfarculus baarsii
?
-
-
-
-
reduced rubredoxin + superoxide + 2 H+
-
715670
Desulfarculus baarsii
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
the mononuclear iron center with an FeN4S1 coordination catalyzes the one electron reduction of superoxide to form hydrogen peroxide in presence of an additional rubredoxin-like desulforedoxin iron center
715670
Desulfarculus baarsii
rubredoxin + H2O2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
three-dimensional structure of the homodimeric SOR, modelling, overview
Desulfarculus baarsii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Desulfarculus baarsii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Desulfarculus baarsii
General Information
General Information
Commentary
Organism
additional information
the SOR active site is located at the surface of the protein and consists of a mononuclear iron center, named center II, pentacoordinated in its ferrous state by four nitrogen atoms from histidine residues in an equatorial plane and one sulfur atom from a cysteine residue in an axial position. It displays a high redox potential. The lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide
Desulfarculus baarsii
physiological function
superoxide reductase, SOR, is a superoxide detoxification system, with a role of the rubredoxin-like iron center in the superoxide detoxifying activity of SOR, overview
Desulfarculus baarsii
General Information (protein specific)
General Information
Commentary
Organism
additional information
the SOR active site is located at the surface of the protein and consists of a mononuclear iron center, named center II, pentacoordinated in its ferrous state by four nitrogen atoms from histidine residues in an equatorial plane and one sulfur atom from a cysteine residue in an axial position. It displays a high redox potential. The lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide
Desulfarculus baarsii
physiological function
superoxide reductase, SOR, is a superoxide detoxification system, with a role of the rubredoxin-like iron center in the superoxide detoxifying activity of SOR, overview
Desulfarculus baarsii
Other publictions for EC 1.15.1.2
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)
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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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4
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1
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1
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743942
Sousa
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Giardia intestinalis
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71
2236-2247
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1
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1
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1
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2
2
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730554
Horch
Reductive activation and struc ...
Ignicoccus hospitalis
Phys. Chem. Chem. Phys.
16
14220-14230
2014
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1
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1
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4
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744022
Bonnot
Formation of high-valent iron ...
Desulfarculus baarsii, Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
Angew. Chem. Int. Ed. Engl.
53
5926-5930
2014
-
-
-
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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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3
3
-
-
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744687
Sheng
Superoxide dismutases and sup ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558, Desulfarculus baarsii, Desulfarculus baarsii ATCC 33931, Desulfovibrio desulfuricans, Desulfovibrio vulgaris, Dosidicus gigas, Ignicoccus hospitalis, Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125, Nanoarchaeum equitans, Pyrococcus furiosus, Pyrococcus furiosus ATCC 43587, Pyrococcus horikoshii, Thermotoga maritima, Thermotoga maritima ATCC 43589, Treponema pallidum, Treponema pallidum Nichols
Chem. Rev.
114
3854-3918
2014
-
-
-
6
13
-
-
-
-
11
-
18
-
19
-
-
-
-
-
-
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-
18
6
-
-
-
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-
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-
6
13
-
-
-
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12
-
18
-
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-
-
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18
6
-
-
-
-
-
-
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-
22
24
-
-
-
746425
Horch
-
Metal-induced histidine depro ...
Ignicoccus hospitalis, Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125
RSC Adv.
4
54091-54095
2014
-
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1
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1
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3
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1
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2
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-
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2
2
-
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-
727313
Almeida
Superoxide reductase: differen ...
Desulfovibrio gigas
ChemBioChem
14
1858-1866
2013
-
-
1
-
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-
1
1
1
2
1
2
-
2
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1
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2
1
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2
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3
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1
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1
3
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1
1
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1
1
2
1
2
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1
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2
1
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2
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2
2
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726989
Caranto
Treponema denticola superoxide ...
Treponema denticola, Treponema denticola 35405
Biochemistry
51
5601-5610
2012
-
-
1
-
1
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2
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2
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3
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4
1
1
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1
1
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1
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2
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2
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1
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4
1
1
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1
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3
3
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-
715670
Bonnot
Intermolecular electron transf ...
Desulfarculus baarsii
J. Biol. Inorg. Chem.
16
889-898
2011
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1
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2
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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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4
1
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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-
4
1
1
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1
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2
2
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-
726902
Folgosa
New spectroscopic and electroc ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
Biochem. J.
438
485-494
2011
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1
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4
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17
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4
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4
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2
2
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727470
Krätzer
Methanoferrodoxin represents a ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
FEBS J.
278
442-451
2011
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1
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1
2
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4
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1
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1
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6
1
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1
1
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727572
Testa
The superoxide reductase from ...
Giardia intestinalis, Giardia intestinalis WB clone C6
Free Radic. Biol. Med.
51
1567-1574
2011
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1
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1
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2
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6
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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
1
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1
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3
3
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746936
Lakhal
Oxygen uptake rates in the hy ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Arch. Microbiol.
193
429-438
2011
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4
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1
1
1
1
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713639
Bandeiras
Purification, crystallization ...
Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
66
316-319
2010
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1
1
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1
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1
1
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713642
Pinho
Cloning, purification, crystal ...
Ignicoccus hospitalis
Acta Crystallogr. Sect. F
66
605-607
2010
-
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1
1
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2
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4
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1
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2
2
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714326
Pinto
Reductive elimination of super ...
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio desulfuricans, Desulfovibrio gigas, Desulfovibrio vulgaris, Nanoarchaeum equitans, Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermotoga maritima, Treponema pallidum
Biochim. Biophys. Acta
1804
285-297
2010
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1
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11
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1
10
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17
9
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4
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7
4
6
7
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1
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10
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11
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1
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17
9
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10
10
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-
714327
Bonnot
Photochemical processes observ ...
Desulfarculus baarsii
Biochim. Biophys. Acta
1804
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2010
-
-
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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2
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1
1
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700630
Todorovic
Resonance Raman study of the s ...
Archaeoglobus fulgidus, Nanoarchaeum equitans
Phys. Chem. Chem. Phys.
11
1809-1815
2009
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-
2
-
2
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5
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2
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723459
Im
Expression of Pyrococcus furio ...
Pyrococcus furiosus
Plant Physiol.
151
893-904
2009
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1
-
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1
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4
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1
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687820
Rodrigues
Superoxide reduction by Nanoar ...
Nanoarchaeum equitans
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13
219-228
2008
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1
-
1
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1
-
1
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1
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1
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2
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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2
1
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-
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674937
Rodrigues
Superoxide reduction by Archae ...
Archaeoglobus fulgidus
J. Biol. Inorg. Chem.
12
248-256
2007
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1
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1
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2
2
1
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1
1
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2
1
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1
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1
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1
1
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2
2
1
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2
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2
1
-
-
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-
1
-
-
-
-
-
-
-
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-
684111
Kovacs
Understanding how the thiolate ...
Desulfarculus baarsii
Acc. Chem. Res.
40
501-509
2007
-
-
-
-
-
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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
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2
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685089
Huang
Reaction of Desulfovibrio vulg ...
Desulfovibrio vulgaris
Biochemistry
46
11342-11351
2007
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-
-
3
-
4
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
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1
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1
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2
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1
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686522
Pereira
-
Superoxide reductases ...
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio desulfuricans, Desulfovibrio gigas, Desulfovibrio vulgaris, Methanothermobacter thermautotrophicus, Pyrococcus furiosus, Thermotoga maritima, Treponema pallidum
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2007
2569-2581
2007
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5
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2
9
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9
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9
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27
11
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9
-
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9
9
5
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10
2
9
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27
11
-
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-
686523
Brines
-
Understanding the mechanism of ...
Desulfarculus baarsii, Desulfovibrio desulfuricans, Pyrococcus furiosus, Treponema palladium
Eur. J. Inorg. Chem.
2007
29-38
2007
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1
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12
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8
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4
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4
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8
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4
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4
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1
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12
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8
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4
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8
-
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686751
Riebe
Desulfoferrodoxin of Clostridi ...
Clostridium acetobutylicum
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581
5605-5610
2007
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1
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1
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2
-
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687278
Dey
Sulfur K-edge X-ray absorption ...
Pyrococcus furiosus
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129
12418-12431
2007
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1
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1
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2
-
-
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-
-
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-
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687582
Mathe
Assessing the role of the acti ...
Desulfarculus baarsii
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282
22207-22216
2007
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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
1
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1
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1
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1
-
1
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-
2
-
-
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-
-
-
-
-
-
-
-
-
-
-
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672207
Rodrigues
Superoxide reduction mechanism ...
Archaeoglobus fulgidus
Biochemistry
45
9266-9278
2006
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-
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-
2
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1
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3
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1
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-
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-
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-
-
-
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-
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672631
Mathe
Fe(3+)-eta(2)-peroxo species i ...
Desulfarculus baarsii, Treponema pallidum
Biophys. Chem.
119
38-48
2006
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674927
Santos-Silva
The first crystal structure of ...
Treponema pallidum
J. Biol. Inorg. Chem.
11
548-558
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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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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676815
Molina-Heredia
Detoxification of superoxide w ...
Desulfarculus baarsii
Proc. Natl. Acad. Sci. USA
103
14750-14755
2006
-
-
-
-
-
-
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1
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2
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1
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-
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-
-
-
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-
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657785
Rodrigues
Rubredoxin acts as an electron ...
Archaeoglobus fulgidus
Biochem. Biophys. Res. Commun.
329
1300-1305
2005
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2
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1
-
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-
-
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-
-
-
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671088
Santos-Silva
Superoxide reductase from the ...
Treponema pallidum
Acta Crystallogr. Sect. F
61
967-970
2005
-
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-
1
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1
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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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673630
Im
Production of a thermostable a ...
Pyrococcus furiosus
FEBS Lett.
579
5521-5526
2005
-
1
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-
1
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3
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1
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-
-
-
-
-
-
-
-
-
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-
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-
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673998
Theisen
Role of protons in superoxide ...
synthetic construct
Inorg. Chem.
44
1169-1171
2005
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-
-
-
-
-
-
-
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1
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-
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1
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-
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
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-
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674155
Mathe
Fe3+-hydroxide ligation in the ...
Desulfarculus baarsii
J. Am. Chem. Soc.
127
16436-16441
2005
-
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-
2
-
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1
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2
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2
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1
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-
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721334
Grunden
In vitro reconstitution of an ...
Pyrococcus furiosus
Appl. Environ. Microbiol.
71
1522-1530
2005
-
-
-
-
-
-
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1
-
4
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1
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2
-
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-
-
-
-
-
-
-
-
-
-
-
658089
Niviere
Superoxide reductase from Desu ...
Desulfarculus baarsii
Biochemistry
43
808-818
2004
-
-
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-
2
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3
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1
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-
-
-
-
-
-
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-
660519
Adam
Structure of superoxide reduct ...
Desulfarculus baarsii
Structure
12
1729-1740
2004
-
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1
1
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3
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1
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1
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660350
Emerson
An engineered two-iron superox ...
Desulfovibrio vulgaris
Proc. Natl. Acad. Sci. USA
100
3802-3807
2003
-
-
-
-
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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-
-
-
-
-
-
-
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-
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-
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1
-
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1
-
1
-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723617
Clay
Nitric oxide binding at the mo ...
Pyrococcus furiosus
Proc. Natl. Acad. Sci. USA
100
3796-3801
2003
-
-
-
-
-
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2
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1
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1
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-
1
-
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-
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-
-
-
-
-
-
-
390156
Clay
Spectroscopic studies of Pyroc ...
Pyrococcus furiosus
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124
788-805
2002
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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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-
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-
-
-
-
-
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-
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-
-
-
-
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390157
Mathe
Identification of iron(III) pe ...
Desulfarculus baarsii
J. Am. Chem. Soc.
124
4966-4967
2002
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1
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2
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1
-
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1
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390159
Rusnak
Superoxide reductase activitie ...
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio vulgaris, Pyrococcus furiosus, Treponema pallidum
Methods Enzymol.
349
243-258
2002
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390160
Niviere
Superoxide reductase from Desu ...
Desulfarculus baarsii, Treponema pallidum
Methods Enzymol.
349
123-129
2002
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390161
Emerson
Kinetics and mechanism of supe ...
Desulfovibrio vulgaris
Biochemistry
41
4348-4357
2002
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657916
Berthomieu
Redox-dependent structural cha ...
Desulfarculus baarsii
Biochemistry
41
10360-10368
2002
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721586
Clay
Resonance Raman characterizati ...
Pyrococcus furiosus
Biochemistry
41
9833-9841
2002
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390153
Lombard
Superoxide reductase from Desu ...
Desulfarculus baarsii
Biochemistry
40
5032-5040
2001
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390154
Coulter
A role for rubredoxin in oxida ...
Desulfovibrio vulgaris
Arch. Biochem. Biophys.
394
76-86
2001
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390155
Lumppio
Rubrerythrin and rubredoxin ox ...
Desulfovibrio vulgaris
J. Bacteriol.
183
101-108
2001
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745202
Adams
Key role for sulfur in peptid ...
Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
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390149
Jovanovic
Neelaredoxin, an iron-binding ...
Treponema pallidum
J. Biol. Chem.
275
28439-28448
2000
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390150
Lombard
Reaction of the desulfoferrodo ...
Desulfarculus baarsii
J. Biol. Chem.
275
115-121
2000
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390151
Abreu
Oxygen detoxification in the s ...
Archaeoglobus fulgidus
Mol. Microbiol.
38
322-334
2000
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390152
Yeh
Structures of the superoxide r ...
Pyrococcus furiosus
Biochemistry
39
2499-2508
2000
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390158
Coulter
-
Superoxide reactivity of rubre ...
Desulfovibrio vulgaris
J. Am. Chem. Soc.
122
11555-11556
2000
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390148
Jenney
Anaerobic microbes: oxygen det ...
Pyrococcus furiosus
Science
286
306-309
1999
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