BRENDA - Enzyme Database show
show all sequences of 1.97.1.9

Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions

Ridley, H.; Watts, C.A.; Richardson, D.J.; Butler, C.S.; Appl. Environ. Microbiol. 72, 5173-5180 (2006)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1
-
selenate
pH 7.2, 30C, holenzyme complex
Enterobacter cloacae
5.5
-
selenate
pH 7.2, 30C, isolated alpha subunit
Enterobacter cloacae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Enterobacter cloacae
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
non-heme iron, 18 mol per mol of enzyme
Enterobacter cloacae
Molybdenum
0.6 mol per mol of enzyme
Enterobacter cloacae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
Enterobacter cloacae
55000
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
Enterobacter cloacae
600000
-
gel filtration
Enterobacter cloacae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Enterobacter cloacae
-
expression under aerobic conditions, poor expression during anaerobic growth on nitrate
-
Enterobacter cloacae SLD1a-1 / ATCC 700258
-
expression under aerobic conditions, poor expression during anaerobic growth on nitrate
-
Purification (Commentary)
Commentary
Organism
-
Enterobacter cloacae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
500
-
pH 7.2, 30C
Enterobacter cloacae
Storage Stability
Storage Stability
Organism
-20C, enzyme extracted with Thesit retains 50% activity after being frozen for prolonged periods
Enterobacter cloacae
4C, enzyme extracted with Thesit remains active for 24 h
Enterobacter cloacae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no substrate: nitrate, sulfate, perchlorate, thiosulfate
671468
Enterobacter cloacae
?
-
-
-
-
additional information
no substrate: nitrate, sulfate, perchlorate, thiosulfate
671468
Enterobacter cloacae SLD1a-1 / ATCC 700258
?
-
-
-
-
selenate + electron donor
-
671468
Enterobacter cloacae
selenite + H2O + oxidized donor
-
-
-
?
selenate + electron donor
-
671468
Enterobacter cloacae SLD1a-1 / ATCC 700258
selenite + H2O + oxidized donor
-
-
-
?
Subunits
Subunits
Commentary
Organism
nonamer
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
Enterobacter cloacae
Cofactor
Cofactor
Commentary
Organism
Structure
heme
0.9 mol per mol of enzyme
Enterobacter cloacae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
0.9 mol per mol of enzyme
Enterobacter cloacae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1
-
selenate
pH 7.2, 30C, holenzyme complex
Enterobacter cloacae
5.5
-
selenate
pH 7.2, 30C, isolated alpha subunit
Enterobacter cloacae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Enterobacter cloacae
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
non-heme iron, 18 mol per mol of enzyme
Enterobacter cloacae
Molybdenum
0.6 mol per mol of enzyme
Enterobacter cloacae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
Enterobacter cloacae
55000
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
Enterobacter cloacae
600000
-
gel filtration
Enterobacter cloacae
Purification (Commentary) (protein specific)
Commentary
Organism
-
Enterobacter cloacae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
500
-
pH 7.2, 30C
Enterobacter cloacae
Storage Stability (protein specific)
Storage Stability
Organism
-20C, enzyme extracted with Thesit retains 50% activity after being frozen for prolonged periods
Enterobacter cloacae
4C, enzyme extracted with Thesit remains active for 24 h
Enterobacter cloacae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no substrate: nitrate, sulfate, perchlorate, thiosulfate
671468
Enterobacter cloacae
?
-
-
-
-
additional information
no substrate: nitrate, sulfate, perchlorate, thiosulfate
671468
Enterobacter cloacae SLD1a-1 / ATCC 700258
?
-
-
-
-
selenate + electron donor
-
671468
Enterobacter cloacae
selenite + H2O + oxidized donor
-
-
-
?
selenate + electron donor
-
671468
Enterobacter cloacae SLD1a-1 / ATCC 700258
selenite + H2O + oxidized donor
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
nonamer
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
Enterobacter cloacae
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
-
-
-
-
-
-
9
2
1
2
1
4
2
2
-
-
1
-
-
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1
-
4
1
1
1
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
2
1
2
1
4
2
-
-
1
-
-
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
-
-
-
-
-
8
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
744808
Wen
Quantitative detection of sel ...
Pseudomonas stutzeri, Thauera selenatis, Thauera selenatis ATCC 55363, Thauera sp.
Enzyme Microb. Technol.
85
19-24
2016
-
-
3
-
3
-
-
-
-
-
-
4
-
7
-
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4
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3
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3
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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
-
5
-
-
-
1
-
-
2
-
4
-
-
-
-
-
-
-
-
2
2
-
-
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1
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5
-
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1
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2
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-
-
2
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
744931
Yee
Selenate reductase activity i ...
Escherichia coli
FEMS Microbiol. Lett.
361
138-143
2014
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
1
1
-
-
-
727752
Kuroda
Molecular cloning and characte ...
Bacillus selenatarsenatis, Bacillus selenatarsenatis SF-1
J. Bacteriol.
193
2141-2148
2011
-
-
1
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
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3
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-
-
-
-
-
-
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-
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1
3
-
-
-
714365
Dridge
Thermostable properties of the ...
Thauera selenatis
Biochimie
92
1268-1273
2010
-
-
-
-
-
-
1
2
-
1
3
-
-
3
-
-
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1
1
2
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1
-
1
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1
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2
-
1
3
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1
1
2
-
1
-
1
-
-
-
-
-
-
-
-
-
715508
Lowe
Quinol-cytochrome c oxidoreduc ...
Thauera selenatis
J. Biol. Chem.
285
18433-18442
2010
-
-
-
-
-
-
-
-
-
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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1
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-
-
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1
-
-
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-
-
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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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-
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1
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2
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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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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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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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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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3
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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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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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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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11
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1
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2
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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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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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644813
Krafft
Cloning and sequencing of the ...
Thauera selenatis
DNA Seq.
10
365-377
2000
-
-
1
-
1
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644812
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Bacterial respiration of arsen ...
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3
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Schroder
Purification and characterizat ...
Thauera selenatis
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1997
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Rech
The terminal reductases for se ...
Thauera selenatis
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