BRENDA - Enzyme Database show
show all sequences of 1.97.1.9

Thermostable properties of the periplasmic selenate reductase from Thauera selenatis

Dridge, E.J.; Butler, C.S.; Biochimie 92, 1268-1273 (2010)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
tungstate
SER isolated from periplasmic fractions from cells grown on 1 mM tungstate display selenate reductase activities with a 20fold reduction in Vmax and a 23fold increase in substrate binding affinity. The thermo-stability and pH dependence of tungsten-SER is shown to be similar to that observed for molybdenum-SER
Thauera selenatis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0007
-
selenate
tungsten-SER, pH and temperature not specified in the publication, Vmax: 0.01 micromol/min/mg
Thauera selenatis
0.016
-
selenate
molybdenum-SER, pH and temperature not specified in the publication, Vmax: 0.2 micromol/min/mg
Thauera selenatis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Molybdenum
-
Thauera selenatis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
23000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
40000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
96000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thauera selenatis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
selenate + reduced methyl viologen
-
714365
Thauera selenatis
selenite + H2O + oxidized methyl viologen
-
-
-
?
Subunits
Subunits
Commentary
Organism
trimer
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
65
-
optimal temperature for molybdenum-SER
Thauera selenatis
80
-
optimal temperature for tungsten-SER is higher than 80C
Thauera selenatis
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
purified molybdenum-SER complex is stable and active upon heat-shock incubation for 10 min at temperatures up to 60C. At temperatures greater than 65C all three subunits (SerABC) are readily denatured
Thauera selenatis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Thauera selenatis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
tungstate
SER isolated from periplasmic fractions from cells grown on 1 mM tungstate display selenate reductase activities with a 20fold reduction in Vmax and a 23fold increase in substrate binding affinity. The thermo-stability and pH dependence of tungsten-SER is shown to be similar to that observed for molybdenum-SER
Thauera selenatis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0007
-
selenate
tungsten-SER, pH and temperature not specified in the publication, Vmax: 0.01 micromol/min/mg
Thauera selenatis
0.016
-
selenate
molybdenum-SER, pH and temperature not specified in the publication, Vmax: 0.2 micromol/min/mg
Thauera selenatis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Molybdenum
-
Thauera selenatis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
23000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
40000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
96000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
selenate + reduced methyl viologen
-
714365
Thauera selenatis
selenite + H2O + oxidized methyl viologen
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
trimer
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Thauera selenatis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
65
-
optimal temperature for molybdenum-SER
Thauera selenatis
80
-
optimal temperature for tungsten-SER is higher than 80C
Thauera selenatis
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
purified molybdenum-SER complex is stable and active upon heat-shock incubation for 10 min at temperatures up to 60C. At temperatures greater than 65C all three subunits (SerABC) are readily denatured
Thauera selenatis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Thauera selenatis
Other publictions for EC 1.97.1.9
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)
745578
Mesbahi-Nowrouzi
-
Purification of selenate redu ...
Alcaligenes sp., Alcaligenes sp. CKCr-6A
J. Mol. Liq.
249
1254-1262
2018
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-
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9
2
1
2
1
4
2
2
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1
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1
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4
1
1
1
1
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1
1
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9
-
2
1
2
1
4
2
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1
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-
1
-
4
1
1
1
1
-
1
1
-
-
-
1
1
-
-
-
744727
Subedi
Simultaneous selenate reducti ...
Clostridium sp., Clostridium ultunense, Exiguobacterium sp., Gottschalkia acidurici, Gottschalkia acidurici ATCC 7906, Lysinibacillus sp., Pseudomonas sp., Thauera sp. MZ1T, Tissierella sp.
Chemosphere
183
536-545
2017
-
8
-
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8
-
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18
-
16
-
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18
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8
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8
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18
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18
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744808
Wen
Quantitative detection of sel ...
Pseudomonas stutzeri, Thauera selenatis, Thauera selenatis ATCC 55363, Thauera sp.
Enzyme Microb. Technol.
85
19-24
2016
-
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3
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3
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4
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7
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4
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4
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745727
Connelly
Biosynthesis of selenate redu ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2a
Microbiology
162
2136-2146
2016
-
-
1
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5
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1
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2
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4
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2
2
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1
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5
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1
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2
2
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1
1
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-
744931
Yee
Selenate reductase activity i ...
Escherichia coli
FEMS Microbiol. Lett.
361
138-143
2014
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2
-
2
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2
1
1
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-
1
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1
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2
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-
2
1
1
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1
1
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727752
Kuroda
Molecular cloning and characte ...
Bacillus selenatarsenatis, Bacillus selenatarsenatis SF-1
J. Bacteriol.
193
2141-2148
2011
-
-
1
-
-
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-
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10
-
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3
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1
3
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-
714365
Dridge
Thermostable properties of the ...
Thauera selenatis
Biochimie
92
1268-1273
2010
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1
2
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1
3
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3
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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
3
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1
1
2
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1
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1
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715508
Lowe
Quinol-cytochrome c oxidoreduc ...
Thauera selenatis
J. Biol. Chem.
285
18433-18442
2010
-
-
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1
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2
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1
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1
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1
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697509
Hunter
Reduction of selenite to eleme ...
Pseudomonas sp., Pseudomonas sp. CA5
Curr. Microbiol.
58
493-498
2009
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1
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2
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1
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697647
Ma
Role of menaquinone biosynthes ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258, Escherichia coli K-12
Environ. Microbiol.
11
149-158
2009
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11
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699361
Leaver
Enterobacter cloacae SLD1a-1 g ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
J. Ind. Microbiol. Biotechnol.
35
867-873
2008
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1
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2
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8
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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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2
1
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1
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684986
Dridge
Investigation of the redox cen ...
Thauera selenatis
Biochem. J.
408
19-28
2007
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1
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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671304
Ridley
Development of a viologen-base ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
Anal. Biochem.
358
289-294
2006
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2
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1
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7
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1
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1
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1
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671468
Ridley
Resolution of distinct membran ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
Appl. Environ. Microbiol.
72
5173-5180
2006
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2
1
2
3
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7
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1
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1
2
4
1
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1
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1
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1
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3
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1
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1
2
4
1
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657903
Watts
Microbial reduction of selenat ...
Enterobacter cloacae, Enterobacter cloacae SLDa-1, Sulfurospirillum barnesii, Thauera selenatis
Biochem. Soc. Trans.
33
173-175
2005
1
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1
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4
3
9
4
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4
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5
2
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1
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1
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1
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4
3
9
4
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5
2
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658902
Maher
X-ray absorption spectroscopy ...
Thauera selenatis
Inorg. Chem.
43
402-404
2004
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2
4
1
1
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2
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1
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1
1
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2
1
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644816
Watts
Selenate reduction by Enteroba ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
FEMS Microbiol. Lett.
228
273-279
2003
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2
2
4
1
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2
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7
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1
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11
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1
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2
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2
4
1
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2
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1
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11
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1
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644814
Maher
Crystallization and preliminar ...
Thauera selenatis
Acta Crystallogr. Sect. D
58
706-708
2002
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1
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3
-
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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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3
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1
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1
1
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644815
Bebien
Involvement of a putative moly ...
Escherichia coli
Microbiology
148
3865-3872
2002
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1
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1
2
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3
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1
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1
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1
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644813
Krafft
Cloning and sequencing of the ...
Thauera selenatis
DNA Seq.
10
365-377
2000
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1
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1
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1
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1
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5
-
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644812
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Bacterial respiration of arsen ...
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Schroder
Purification and characterizat ...
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1997
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Rech
The terminal reductases for se ...
Thauera selenatis
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