BRENDA - Enzyme Database show
show all sequences of 1.8.5.3

Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion

Tang, H.; Rothery, R.A.; Voss, J.E.; Weiner, J.H.; J. Biol. Chem. 286, 15147-15154 (2011)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
DELTAN21
mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
Escherichia coli
R61K
molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
Escherichia coli
V20Y/DELTAN21/P27G
introduction of a type I Cys group, mutations eliminate both molybdo-bis(pyranopterin guanine dinucleotide) binding and detection of a FSo cluster by EPR
Escherichia coli
V20Y/DELTAN21/P27G/R61K
addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P18775
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.07
-
mutant DELTAN21, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
0.14
-
mutant V20Y/DELTAN21/P27G, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
0.33
-
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
2.63
-
mutant R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
5.22
-
mutant V20Y/DELTAN21/P27G, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
5.91
-
mutant DELTAN21, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
7.72
-
wild-type, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
7.97
-
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
125
-
mutant R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
141
-
wild-type, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
trimethylamine N-oxide + reduced benzyl viologen
-
725419
Escherichia coli
trimethylamine + oxidized benzyl viologen
-
-
-
?
trimethylamine N-oxide + reduced lapachol
-
725419
Escherichia coli
trimethylamine + oxidized lapachol
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
[4Fe-4S]-center
role for the cluster in directing molybdenum cofactor assembly during enzyme maturation. The cluster is predicted to be in close proximity to the molybdo-bis(pyranopterin guanine dinucleotide) cofactor, which provides the site of dimethyl sulfoxide reduction
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
[4Fe-4S]-center
role for the cluster in directing molybdenum cofactor assembly during enzyme maturation. The cluster is predicted to be in close proximity to the molybdo-bis(pyranopterin guanine dinucleotide) cofactor, which provides the site of dimethyl sulfoxide reduction
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
DELTAN21
mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
Escherichia coli
R61K
molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
Escherichia coli
V20Y/DELTAN21/P27G
introduction of a type I Cys group, mutations eliminate both molybdo-bis(pyranopterin guanine dinucleotide) binding and detection of a FSo cluster by EPR
Escherichia coli
V20Y/DELTAN21/P27G/R61K
addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.07
-
mutant DELTAN21, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
0.14
-
mutant V20Y/DELTAN21/P27G, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
0.33
-
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
2.63
-
mutant R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
5.22
-
mutant V20Y/DELTAN21/P27G, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
5.91
-
mutant DELTAN21, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
7.72
-
wild-type, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
Escherichia coli
7.97
-
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
125
-
mutant R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
141
-
wild-type, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
trimethylamine N-oxide + reduced benzyl viologen
-
725419
Escherichia coli
trimethylamine + oxidized benzyl viologen
-
-
-
?
trimethylamine N-oxide + reduced lapachol
-
725419
Escherichia coli
trimethylamine + oxidized lapachol
-
-
-
?
Other publictions for EC 1.8.5.3
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)
742743
Ha
Sulfur K-edge X-ray absorptio ...
Escherichia coli
J. Am. Chem. Soc.
136
9094-9105
2014
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1
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1
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724457
Tang
A variant conferring cofactor- ...
Escherichia coli
Biochim. Biophys. Acta
1827
730-737
2013
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1
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2
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2
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725605
Li
Large density-functional and b ...
Rhodobacter capsulatus
J. Chem. Theory Comput.
9
1799-1807
2013
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725419
Tang
Correct assembly of iron-sulfu ...
Escherichia coli
J. Biol. Chem.
286
15147-15154
2011
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4
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1
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10
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2
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1
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4
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10
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2
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724687
Hernandez-Marin
-
A kinetic study of dimethyl su ...
Rhodobacter capsulatus
Can. J. Chem.
88
683-693
2010
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1
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712155
George
X-ray absorption spectroscopic ...
Escherichia coli
Inorg. Chem.
46
2-4
2007
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1
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1
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3
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712156
George
Interaction of product analogu ...
Rhodobacter sphaeroides
Inorg. Chem.
46
3097-3104
2007
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1
1
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711196
Cheng
Investigation of the environme ...
Escherichia coli
Biochemistry
44
8068-8077
2005
-
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-
32
-
1
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2
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32
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711815
McNamara
-
The nature and function of the ...
synthetic construct
Dalton Trans.
2005
3572-3579
2005
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2
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1
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712000
Ridge
The critical role of tryptopha ...
Rhodobacter capsulatus
FEBS Lett.
563
197-202
2004
-
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1
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4
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2
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2
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4
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1
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1
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1
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4
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2
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4
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4
4
712148
Baltes
Identification of dimethyl sul ...
Actinobacillus pleuropneumoniae, Actinobacillus pleuropneumoniae serotype 7
Infect. Immun.
71
6784-6792
2003
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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
1
1
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711193
Bray
Reactions of dimethylsulfoxide ...
Rhodobacter capsulatus
Biochemistry
40
9810-9820
2001
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1
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1
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712347
Johnson
An active site tyrosine influe ...
Rhodobacter sphaeroides
J. Biol. Chem.
276
13178-13185
2001
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1
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2
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12
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3
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4
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12
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1
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12
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4
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12
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12
12
712734
Stewart
Dimethylsulfoxide reductase: a ...
Rhodobacter capsulatus
J. Mol. Biol.
299
593-600
2000
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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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711190
Adams
Reactions of dimethylsulfoxide ...
Rhodobacter capsulatus
Biochemistry
38
8501-8511
1999
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2
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5
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5
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3
2
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712341
Rothery
Interactions between the molyb ...
Escherichia coli
J. Biol. Chem.
274
13002-13009
1999
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3
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2
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711886
Simala-Grant
Modulation of the substrate sp ...
Escherichia coli
Eur. J. Biochem.
251
510-515
1998
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15
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28
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4
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3
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30
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15
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28
-
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3
-
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30
-
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-
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25
25
712339
Zhao
Interaction of 2-n-heptyl-4-hy ...
Escherichia coli
J. Biol. Chem.
273
20758-20763
1998
-
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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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712960
Hanlon
Asymmetric reduction of racemi ...
Escherichia coli, Proteus mirabilis, Rhodobacter capsulatus
Microbiology
144
2247-2253
1998
-
-
-
-
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3
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20
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20
-
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711885
Solomon
Characterisation of the pterin ...
Rhodobacter capsulatus
Eur. J. Biochem.
246
200-203
1997
-
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2
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1
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1
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713451
Turner
Expression and epitope tagging ...
Escherichia coli
Protein Eng.
10
285-290
1997
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1
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1
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1
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675504
Schneider
Crystal structure of dimethyl ...
Rhodobacter capsulatus
J. Mol. Biol.
263
53-69
1996
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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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1
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1
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710991
Hilton
Identification of the molybden ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides f. sp. denitrificans
Arch. Biochem. Biophys.
325
139-143
1996
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3
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1
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712959
Simala-Grant
Kinetic analysis and substrate ...
Escherichia coli
Microbiology
142
3231-3239
1996
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20
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2
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25
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25
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20
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25
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25
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1
1
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20
20
713506
Schindelin
Crystal structure of DMSO redu ...
Rhodobacter sphaeroides
Science
272
1615-1621
1996
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1
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2
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1
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1
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711479
Abo
Enantioselective deoxygenation ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides f.s. denitrificans
Bioorg. Med. Chem.
3
109-112
1995
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4
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14
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14
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710783
Fischer
Molybdenum-pterin complexes: A ...
synthetic construct
Adv. Exp. Med. Biol.
338
369-372
1993
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1
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713250
Masui
-
Accumulation on the cytoplasmi ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides f. sp. denitrificans
Plant Cell Physiol.
33
463-469
1992
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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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711803
Miguel
-
Electron donors and the quinon ...
Escherichia coli
Curr. Microbiol.
22
109-115
1991
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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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712043
Daruwala
Dimethyl sulfoxide reductase i ...
Escherichia coli
FEMS Microbiol. Lett.
83
255-259
1991
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2
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1
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1
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1
1
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712267
Sambasivarao
Dimethyl sulfoxide reductase o ...
Escherichia coli
J. Bacteriol.
173
5935-5943
1991
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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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1
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1
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