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(ethylsulfinyl)benzene + reduced benzyl viologen
(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
(methylsulfinyl)benzene + reduced benzyl viologen
(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen
(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
(propylsulfanyl)benzene + reduced benzyl viologen
(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
(S)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(S)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(S)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
catalyses the selective removal of (S)-methyl p-tolyl sulfoxide from a racemic mixture of methyl p-tolyl sulfoxide, resulting in an 88 O/o recovery of enantiomerically pure (R)-methyl p-tolyl sulfoxide
-
-
?
(S)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
1-bromo-4-(methylsulfinyl)benzene + reduced benzyl viologen
1-bromo-4-(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
180% of the rate with dimethysulfoxide
-
-
?
1-methyl-4-(methylsulfinyl)benzene + reduced benzyl viologen
1-methyl-4-(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
150% of the rate with dimethysulfoxide
-
-
?
2-carboxypyridine N-oxide + reduced benzyl viologen + H2O
2-carboxypyridine + oxidized benzyl viologen
-
-
-
-
?
2-chloropyridine N-oxide + reduced benzyl viologen + H2O
2-chloropyridine + oxidized benzyl viologen
-
-
-
-
?
2-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
2-hydroxymethylpyridine + oxidized benzyl viologen
-
-
-
-
?
2-mercaptopyridine N-oxide + reduced benzyl viologen + H2O
2-mercaptopyridine + oxidized benzyl viologen
-
-
-
-
?
2-methylpyridine N-oxide + reduced benzyl viologen + H2O
2-methylpyridine + oxidized benzyl viologen
-
-
-
-
?
3-amidopyridine N-oxide + reduced benzyl viologen + H2O
3-amidopyridine + oxidized benzyl viologen
-
-
-
-
?
3-carboxypyridine N-oxide + reduced benzyl viologen + H2O
3-carboxypyridine + oxidized benzyl viologen
-
-
-
-
?
3-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
3-hydroxymethylpyridine + oxidized benzyl viologen
-
-
-
-
?
3-hydroxypyridine N-oxide + reduced benzyl viologen + H2O
3-hydroxypyridine + oxidized benzyl viologen
-
-
-
-
?
3-methylpyridine N-oxide + reduced benzyl viologen + H2O
3-methylpyridine + oxidized benzyl viologen
-
-
-
-
?
3alpha-hydroxybenzylpyridine N-oxide + reduced benzyl viologen + H2O
3alpha-hydroxybenzylpyridine + oxidized benzyl viologen
-
-
-
-
?
4-carboxypyridine N-oxide + reduced benzyl viologen + H2O
4-carboxypyridine + oxidized benzyl viologen
-
-
-
-
?
4-chloropyridine N-oxide + reduced benzyl viologen + H2O
4-chloropyridine + oxidized benzyl viologen
-
-
-
-
?
4-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
4-hydroxymethylpyridine + oxidized benzyl viologen
-
-
-
-
?
4-methylmorpholine N-oxide + reduced benzyl viologen + H2O
4-methylmorpholine + oxidized benzyl viologen
-
-
-
-
?
4-methylpyridine N-oxide + reduced benzyl viologen + H2O
4-methylpyridine + oxidized benzyl viologen
-
-
-
-
?
4-phenylpyridine N-oxide + reduced benzyl viologen + H2O
4-phenylpyridine + oxidized benzyl viologen
-
-
-
-
?
adenosine-1N-oxide + reduced dichlorophenolindophenol
adenine + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
dimethyl sulfoxide + reduced methyl viologen
dimethyl sulfide + H2O + oxidized methyl viologen
-
-
-
r
dimethyldodecylamine N-oxide + reduced benzyl viologen + H2O
dimethyldodecylamine + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfide + H2O + oxidized benzyl viologen
dimethylsulfoxide + reduced benzyl viologen
-
-
-
-
r
dimethylsulfide + H2O + oxidized methyl viologen
dimethylsulfoxide + reduced methyl viologen
-
-
-
-
r
dimethylsulfide + H2O + pyridine N-oxide
dimethylsulfoxide + pyridine
-
-
-
-
?
dimethylsulfide + menaquinone + H2O
dimethylsulfoxide + menaquinol
-
-
-
?
dimethylsulfoxide + 2,3-dimethyl-1,4-napthoquinol
dimethylsulfide + H2O + 2,3-dimethyl-1,4-napthoquinone
-
-
-
-
r
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
dimethylsulfoxide + reduced benzyl viologen + H2O
dimethylsulfide + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfoxide + reduced dichlorophenolindophenol
dimethylsulfide + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
dimethylsulfoxide + reduced methyl viologen
dimethylsulfide + H2O + oxidized methyl viologen
-
-
-
-
r
dithane 1-oxide + reduced benzyl viologen + H2O
dithane + oxidized benzyl viologen
-
-
-
-
?
DL-methyl phenyl sulfoxide + reduced benzyl viologen + H2O
DL-methyl phenyl sulfide + oxidized benzyl viologen
-
-
-
-
?
methionine sulfoxide + reduced benzyl viologen + H2O
methionine + oxidized benzyl viologen
-
-
-
-
?
methionine sulfoxide + reduced dichlorophenolindophenol
methionine + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
pyridine N-oxide + reduced benzyl viologen + H2O
pyridine + oxidized benzyl viologen
-
-
-
-
?
tetramethylene sulfoxide + reduced benzyl viologen + H2O
tetramethylene sulfide + oxidized benzyl viologen
-
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen
trimethylamine + oxidized benzyl viologen
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen + H2O
trimethylamine + oxidized benzyl viologen
-
-
-
-
?
trimethylamine N-oxide + reduced dichlorophenolindophenol
trimethylamine + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
trimethylamine N-oxide + reduced lapachol
trimethylamine + oxidized lapachol
-
-
-
?
trimethylamine-N-oxide + reduced methyl viologen
trimethylamine + H2O + oxidized methyl viologen
-
-
-
-
r
[(methylsulfinyl)methyl]benzene + reduced benzyl viologen
[(methylsulfanyl)methyl]benzene + H2O + oxidized benzyl viologen
-
130% of the rate with dimethysulfoxide
-
-
?
additional information
?
-
(ethylsulfinyl)benzene + reduced benzyl viologen

(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
90% of the rate with dimethysulfoxide
-
-
?
(ethylsulfinyl)benzene + reduced benzyl viologen
(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
Luteovulum sphaeroides f.s. denitrificans
-
90% of the rate with dimethysulfoxide
-
-
?
(methylsulfinyl)benzene + reduced benzyl viologen

(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
150% of the rate with dimethysulfoxide
-
-
?
(methylsulfinyl)benzene + reduced benzyl viologen
(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
Luteovulum sphaeroides f.s. denitrificans
-
150% of the rate with dimethysulfoxide
-
-
?
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen

(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
35% of the rate with dimethysulfoxide
-
-
?
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen
(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
Luteovulum sphaeroides f.s. denitrificans
-
35% of the rate with dimethysulfoxide
-
-
?
(propylsulfanyl)benzene + reduced benzyl viologen

(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
-
35% of the rate with dimethysulfoxide
-
-
?
(propylsulfanyl)benzene + reduced benzyl viologen
(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
Luteovulum sphaeroides f.s. denitrificans
-
35% of the rate with dimethysulfoxide
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O

ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O

methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O

methyl p-tolyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O

methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
dimethylsulfoxide + reduced benzyl viologen

dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
r
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
r
additional information

?
-
-
enzyme catalyses the enantioselective reduction of (R)-sulfoxides
-
-
?
additional information
?
-
-
for the reduction of dimethylsulfoxide, NADH, formate, lactate, reduced benzyl viologen, reduced methyl viologen, and dithionite can serve as electron donors. Menaquinone is involved in electron transport during dimethylsulfoxide reduction
-
-
?
additional information
?
-
-
for all substrates studied, enzyme catalyzes deoxygenation of (S)-sulfoxides predominantly
-
-
?
additional information
?
-
Luteovulum sphaeroides f.s. denitrificans
-
for all substrates studied, enzyme catalyzes deoxygenation of (S)-sulfoxides predominantly
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (R)-sulfoxides
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (R)-sulfoxides
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (S)-sulfoxides
-
-
?
additional information
?
-
formation of the intermediate formed by reaction of DMSOR with dimethylsulfide occurs at a redox potential that is 80 mV higher than that required for reduction of Mo(VI) to Mo(IV) in the free enzyme. In the back-assay the Mo(IV) state may at least in part be by-passed via two successive one electron-reactions of the intermediate with the electron-acceptor
-
-
?
additional information
?
-
-
formation of the intermediate formed by reaction of DMSOR with dimethylsulfide occurs at a redox potential that is 80 mV higher than that required for reduction of Mo(VI) to Mo(IV) in the free enzyme. In the back-assay the Mo(IV) state may at least in part be by-passed via two successive one electron-reactions of the intermediate with the electron-acceptor
-
-
?
additional information
?
-
-
Second-order rate constants for the two-electron reduction and reoxidation reactions at pH 5.5 are 190000 and 430 per M and s, respectively, while at pH 8.0, the catalytic step is rate-limiting. Kinetically, for the two-electron reactions, the enzyme is more effective in dimethylsulfide oxidation than in dimethylsulfoxide reduction. Reduction of DMSOR by dimethylsulfide is incomplete below 1 mM dimethylsulfide but complete at higher concentrations. Reoxidation of the dimethylsulfide-reduced state by dimethylsulfoxide is always incomplete
-
-
?
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0.043
2-chloropyridine N-oxide
-
pH 7.0, 30ưC
0.092
2-methylpyridine N-oxide
-
pH 7.0, 30ưC
0.045
3-amidopyridine N-oxide
-
pH 7.0, 30ưC
4.94
3-carboxypyridine N-oxide
-
pH 7.0, 30ưC
0.094
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
3.17
3-hydroxypyridine N-oxide
-
pH 7.0, 30ưC
0.089
3-methylpyridine N-oxide
-
pH 7.0, 30ưC
0.158
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30ưC
0.513
4-chloropyridine N-oxide
-
pH 7.0, 30ưC
0.372
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
11.1
4-methylmorpholine N-oxide
-
pH 7.0, 30ưC
0.452
4-methylpyridine N-oxide
-
pH 7.0, 30ưC
0.246
4-phenylpyridine N-oxide
-
pH 7.0, 30ưC
0.02 - 0.52
adenosine-1N-oxide
0.83
dimethyldodecylamine N-oxide
-
pH 7.0, 30ưC
0.007 - 0.4
Dimethylsulfoxide
0.21
DL-methyl phenyl sulfoxide
-
pH 7.0, 30ưC
0.09 - 19
methionine sulfoxide
0.001 - 3.8
Pyridine N-oxide
0.001 - 1.1
reduced benzyl viologen
0.06
tetramethylene sulfoxide
-
pH 7.0, 30ưC
2.3 - 88
Trimethylamine N-oxide
0.0959 - 0.193
Trimethylamine-N-oxide
0.02
adenosine-1N-oxide

-
wild-type, pH 8.0, temperature not specified in the publication
0.08
adenosine-1N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
0.52
adenosine-1N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.007
Dimethylsulfoxide

-
wild-type, pH 8.0, temperature not specified in the publication
0.0097
Dimethylsulfoxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0261
Dimethylsulfoxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
0.18
Dimethylsulfoxide
-
pH 7.0, 30ưC
0.18
Dimethylsulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.4
Dimethylsulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
0.09
methionine sulfoxide

-
pH 7.0, 30ưC
0.33
methionine sulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
16
methionine sulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
19
methionine sulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.001
Pyridine N-oxide

-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
0.024
Pyridine N-oxide
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
0.028
Pyridine N-oxide
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
0.034
Pyridine N-oxide
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
0.048
Pyridine N-oxide
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
0.048
Pyridine N-oxide
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
0.076
Pyridine N-oxide
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
0.094
Pyridine N-oxide
-
pH 7.0, 30ưC
0.095
Pyridine N-oxide
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
0.1
Pyridine N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.11
Pyridine N-oxide
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
0.12
Pyridine N-oxide
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
0.12
Pyridine N-oxide
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
0.14
Pyridine N-oxide
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
0.18
Pyridine N-oxide
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
0.24
Pyridine N-oxide
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
3.8
Pyridine N-oxide
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
0.001
reduced benzyl viologen

-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
0.019
reduced benzyl viologen
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
0.019
reduced benzyl viologen
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
0.02
reduced benzyl viologen
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
0.023
reduced benzyl viologen
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
0.024
reduced benzyl viologen
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
0.028
reduced benzyl viologen
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
0.032
reduced benzyl viologen
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.033
reduced benzyl viologen
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
0.038
reduced benzyl viologen
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
0.038
reduced benzyl viologen
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
0.039
reduced benzyl viologen
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
0.04
reduced benzyl viologen
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
0.076
reduced benzyl viologen
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
0.11
reduced benzyl viologen
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
1.1
reduced benzyl viologen
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
2.3
Trimethylamine N-oxide

-
mutant Y114A, pH 8.0, temperature not specified in the publication
20.2
Trimethylamine N-oxide
-
pH 7.0, 30ưC
68
Trimethylamine N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
88
Trimethylamine N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.0959
Trimethylamine-N-oxide

-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
0.193
Trimethylamine-N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8
2-carboxypyridine N-oxide
-
pH 7.0, 30ưC
307
2-chloropyridine N-oxide
-
pH 7.0, 30ưC
89.3
2-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
8
2-mercaptopyridine N-oxide
-
pH 7.0, 30ưC
247
2-methylpyridine N-oxide
-
pH 7.0, 30ưC
237
3-amidopyridine N-oxide
-
pH 7.0, 30ưC
168
3-carboxypyridine N-oxide
-
pH 7.0, 30ưC
214
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
429
3-hydroxypyridine N-oxide
-
pH 7.0, 30ưC
231
3-methylpyridine N-oxide
-
pH 7.0, 30ưC
229
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30ưC
30.3
4-carboxypyridine N-oxide
-
pH 7.0, 30ưC
212
4-chloropyridine N-oxide
-
pH 7.0, 30ưC
226
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
573
4-methylmorpholine N-oxide
-
pH 7.0, 30ưC
268
4-methylpyridine N-oxide
-
pH 7.0, 30ưC
297
4-phenylpyridine N-oxide
-
pH 7.0, 30ưC
110 - 2200
adenosine-1N-oxide
21 - 470
dimethyl sulfoxide
239
dimethyldodecylamine N-oxide
-
pH 7.0, 30ưC
8
Dimethylsulfide
-
pH 8.0, 25ưC
7 - 180
Dimethylsulfoxide
28.4
dithane 1-oxide
-
pH 7.0, 30ưC
99.6
DL-methyl phenyl sulfoxide
-
pH 7.0, 30ưC
58 - 180
methionine sulfoxide
14 - 370
reduced benzyl viologen
27
reduced methyl viologen
-
pH 8.0, 25ưC
119
tetramethylene sulfoxide
-
pH 7.0, 30ưC
1203 - 4300
Trimethylamine N-oxide
11.3 - 134.5
Trimethylamine-N-oxide
110
adenosine-1N-oxide

-
wild-type, pH 8.0, temperature not specified in the publication
1200
adenosine-1N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
2200
adenosine-1N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
21
dimethyl sulfoxide

enzyme Mo-DMSOR with molybdenum in the catalytic centre, pH not specified in the publication, temperature not specified in the publication
470
dimethyl sulfoxide
enzyme W-DMSOR with tungsten in the catalytic centre, pH not specified in the publication, temperature not specified in the publication
7
Dimethylsulfoxide

-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
42.9
Dimethylsulfoxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
50
Dimethylsulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
67
Dimethylsulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
79.9
Dimethylsulfoxide
-
pH 7.0, 30ưC
180
Dimethylsulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
58
methionine sulfoxide

-
wild-type, pH 8.0, temperature not specified in the publication
61.1
methionine sulfoxide
-
pH 7.0, 30ưC
92
methionine sulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
180
methionine sulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
3 - 6
Pyridine N-oxide

-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
10
Pyridine N-oxide
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
33
Pyridine N-oxide
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
41
Pyridine N-oxide
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
95
Pyridine N-oxide
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
96
Pyridine N-oxide
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
99
Pyridine N-oxide
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
99
Pyridine N-oxide
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
100
Pyridine N-oxide
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
110
Pyridine N-oxide
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
120
Pyridine N-oxide
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
190
Pyridine N-oxide
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
190
Pyridine N-oxide
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
200
Pyridine N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
243
Pyridine N-oxide
-
pH 7.0, 30ưC
260
Pyridine N-oxide
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
940
Pyridine N-oxide
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
14
reduced benzyl viologen

-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
17
reduced benzyl viologen
-
pH 8.0, 25ưC
17
reduced benzyl viologen
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
19
reduced benzyl viologen
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
23
reduced benzyl viologen
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
24
reduced benzyl viologen
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
27
reduced benzyl viologen
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
39
reduced benzyl viologen
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
46
reduced benzyl viologen
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
47
reduced benzyl viologen
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
55
reduced benzyl viologen
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
60
reduced benzyl viologen
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
61
reduced benzyl viologen
-
wild-type, pH not specified in the publication, temperature not specified in the publication
68
reduced benzyl viologen
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
110
reduced benzyl viologen
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
210
reduced benzyl viologen
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
370
reduced benzyl viologen
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
1203
Trimethylamine N-oxide

-
pH 7.0, 30ưC
1900
Trimethylamine N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
2300
Trimethylamine N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
4300
Trimethylamine N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
11.3
Trimethylamine-N-oxide

-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
134.5
Trimethylamine-N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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7130
2-chloropyridine N-oxide
-
pH 7.0, 30ưC
2690
2-methylpyridine N-oxide
-
pH 7.0, 30ưC
5280
3-amidopyridine N-oxide
-
pH 7.0, 30ưC
34
3-carboxypyridine N-oxide
-
pH 7.0, 30ưC
2280
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
135
3-hydroxypyridine N-oxide
-
pH 7.0, 30ưC
2600
3-methylpyridine N-oxide
-
pH 7.0, 30ưC
1450
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30ưC
413
4-chloropyridine N-oxide
-
pH 7.0, 30ưC
607
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30ưC
52
4-methylmorpholine N-oxide
-
pH 7.0, 30ưC
592
4-methylpyridine N-oxide
-
pH 7.0, 30ưC
1205
4-phenylpyridine N-oxide
-
pH 7.0, 30ưC
4200 - 15000
adenosine-1N-oxide
287
dimethyldodecylamine N-oxide
-
pH 7.0, 30ưC
170 - 7100
Dimethylsulfoxide
483
DL-methyl phenyl sulfoxide
-
pH 7.0, 30ưC
5.8 - 663
methionine sulfoxide
33 - 10000
Pyridine N-oxide
50 - 23300
reduced benzyl viologen
2080
tetramethylene sulfoxide
-
pH 7.0, 30ưC
34 - 830
Trimethylamine N-oxide
100 - 700
Trimethylamine-N-oxide
4200
adenosine-1N-oxide

-
mutant Y114F, pH 8.0, temperature not specified in the publication
5500
adenosine-1N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
15000
adenosine-1N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
170
Dimethylsulfoxide

-
mutant Y114A, pH 8.0, temperature not specified in the publication
300
Dimethylsulfoxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
455
Dimethylsulfoxide
-
pH 7.0, 30ưC
1000
Dimethylsulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
4400
Dimethylsulfoxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
7100
Dimethylsulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
5.8
methionine sulfoxide

-
mutant Y114A, pH 8.0, temperature not specified in the publication
9.5
methionine sulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
180
methionine sulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
663
methionine sulfoxide
-
pH 7.0, 30ưC
33
Pyridine N-oxide

-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
810
Pyridine N-oxide
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
850
Pyridine N-oxide
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
1000
Pyridine N-oxide
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
1100
Pyridine N-oxide
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
1100
Pyridine N-oxide
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
1100
Pyridine N-oxide
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
1200
Pyridine N-oxide
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
1200
Pyridine N-oxide
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
1300
Pyridine N-oxide
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
2000
Pyridine N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2100
Pyridine N-oxide
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
2100
Pyridine N-oxide
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
2580
Pyridine N-oxide
-
pH 7.0, 30ưC
4000
Pyridine N-oxide
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
4000
Pyridine N-oxide
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
10000
Pyridine N-oxide
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
50
reduced benzyl viologen

-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
370
reduced benzyl viologen
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
760
reduced benzyl viologen
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
900
reduced benzyl viologen
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
960
reduced benzyl viologen
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
1000
reduced benzyl viologen
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
1300
reduced benzyl viologen
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
1360
reduced benzyl viologen
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
1600
reduced benzyl viologen
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
1600
reduced benzyl viologen
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
1900
reduced benzyl viologen
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
1900
reduced benzyl viologen
-
wild-type, pH not specified in the publication, temperature not specified in the publication
3300
reduced benzyl viologen
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
3400
reduced benzyl viologen
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
5500
reduced benzyl viologen
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
23300
reduced benzyl viologen
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
34
Trimethylamine N-oxide

-
wild-type, pH 8.0, temperature not specified in the publication
49
Trimethylamine N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
59
Trimethylamine N-oxide
-
pH 7.0, 30ưC
830
Trimethylamine N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
100
Trimethylamine-N-oxide

-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
700
Trimethylamine-N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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A181T
-
mutation in subunit DmsA. About 300% of wild-type catalytic efficiency
C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. The midpoint potential of FS4[3Fe-4S] is insensitive to inhibitor 2-n-heptyl-4-hydroxyquinoline N-oxide as well as to changes in pH from 5 to 7
C38S
-
the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is significantly modified in DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA. In ferricyanide-oxidized glycerol-inhibited DmsAC38SBC, there is no detectable interaction between the oxidized [3Fe-4S] cluster and the molybdo bis(molybdopterin guanine dinucleotide) cofactor
C59S
mutantion renders enzyme maturation sensitive to molybdenum cofactor availability. Residue C59 is a ligand to the FS0 [4Fe-4S] cluster. In the presence of trace amounts of molybdate, the C59S variant assembles normally to the cytoplasmic membrane and supports respiratory growth on DMSO, although the ground state of FS0 as determined by EPR is converted from high-spin, S = 3/2, to low-spin, S = 1/2. In the presence of the molybdenum antagonist tungstate, wild-type enzyme lacks molybdo-bis(pyranopterin guanine dinucleotide), but is translocated via the Tat translocon and assembles on the periplasmic side of the membrane as an apoenzyme. The C59S variant cannot overcome the dual insults of amino acid substitution plus lack of molybdo-bis(pyranopterin guanine dinucleotide) , leading to degradation of the DmsABC subunits
D95A
-
mutation in electron transfer subunit DmsB
D95A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D95K/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D97A
-
mutation in electron transfer subunit DmsB
D97A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
DELTAN21
mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
G190D
-
mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
G190V
-
mutation in subunit DmsA. About 180% of wild-type catalytic efficiency
H106A
-
mutation in electron transfer subunit DmsB
H106A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106E
-
mutation in electron transfer subunit DmsB
H106E/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106I/C102S 2
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H65R
-
mutation in subunit DmsC. Mutant blocks binding of the menaquinol analogue 2-n-heptyl-4-hydroxyquinoline-N-oxide to the protein
H85F
-
mutation in electron transfer subunit DmsB
H85F/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H85T
-
mutation in electron transfer subunit DmsB
H85T/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
K77A
-
mutation in electron transfer subunit DmsB
K77A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
M147I
-
mutation in subunit DmsA. About 65% of wild-type catalytic efficiency
M147L
-
mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
P80A
-
mutation in electron transfer subunit DmsB
P80A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
P80D
-
mutation in electron transfer subunit DmsB
P80H
-
mutation in electron transfer subunit DmsB
R103A
-
mutation in electron transfer subunit DmsB
R103A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
R149C
-
mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
R61K
molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
R77S
-
DmsA-R77S mutant, the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is eliminated
S176A/C102S
-
double mutant DmsA-S176A and DmsB-C102S, contains an engineered [3Fe-4S] cluster in DmsB, no significant paramagnetic interaction is detected between the oxidized [3Fe-4S] cluster and the Mo(V)
S81G
-
mutation in electron transfer subunit DmsB
S81H
-
mutation in electron transfer subunit DmsB
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
V20Y/DELTAN21/P27G/R61K
addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
W191G
-
mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
W357C
-
mutation in subunit DmsA. About 100% of wild-type catalytic efficiency
W357F
-
mutation in subunit DmsA. About 40% of wild-type catalytic efficiency
W357Y
-
mutation in subunit DmsA. About 60% of wild-type catalytic efficiency
Y104A
-
mutation in electron transfer subunit DmsB
Y104A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104D
-
mutation in electron transfer subunit DmsB
Y104D/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 150 mV. The midpoint potential of FS4 increases in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide and decreasing pH
Y104D/H106F/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104E
-
mutation in electron transfer subunit DmsB
Y104E/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 145 mV
Y114A
-
mutation in direction of the active site of trimethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
Y114F
-
mutation in direction of the active site of tiomethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
W116F
-
residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm
A178Q

-
mutation in subunit DmsA. About 1200% of wild-type catalytic efficiency
A178Q
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
G167N

-
mutation in subunit DmsA. About 20% of wild-type catalytic efficiency
G167N
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
Q179I

-
mutation in subunit DmsA. About 500% of wild-type catalytic efficiency
Q179I
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
R217Q

-
mutation in subunit DmsA. About 2.7% of wild-type catalytic efficiency
R217Q
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
T148S

-
mutation in subunit DmsA. About 150% of wild-type catalytic efficiency
T148S
-
mutation in subunit DmsA. Mutant shows altered kinetic parameters for pyridine N-oxide and dimethylsulfoxide, with Km and kcat decreasing and increasing approximately fourfold,respectively
additional information

-
construction of a number of strains lacking portions of the chromosomal dmsABC operon. The mutant strains fail to grow anaerobically on glycerol minimal medium with dimethyl sulfoxide as the sole terminal oxidant but exhibit normal growth with nitrate, fumarate, and trimethylamine N-oxide. In vivo complementation of the mutant with plasmids carrying various dms genes, singly or in combination, reveal that the expression of all three subunits is essential to restore anaerobic growth. Expression of the DmsAB subunits without DmsC results in accumulation of the catalytically active dimer in the cytoplasm. The dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Dimethylnaphthoquinol is oxidized only by the holoenzyme. Results suggest that the membrane-intrinsic subunit is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer
additional information
-
overexpression of a subunit DmsC-dystrophin-specific amino acid sequence construct is toxic to Escherichia coli cells. Toxicity may be overcome by expression in a F0F1-ATPase mutant strain. Overexpression in COS-1 or McA-RH777 cells is not toxic and protein is localized to the endoplasmic reticulum
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Schneider, F.; Lowe, F.; Huber, R.; Schindelin, H.; Kisker, C.; Knablein, J.
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Ang resolution
J. Mol. Biol.
263
53-69
1996
Rhodobacter capsulatus
brenda
Fischer, B.; Schmalle, H.; Dubler, E.; Viscontini, M.
Molybdenum-pterin complexes: A functional and structural model for the binding site in the enzyme dimethyl sulfoxide reductase
Adv. Exp. Med. Biol.
338
369-372
1993
synthetic construct
brenda
Hilton, J.; Rajagopalan, K.
Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum
Arch. Biochem. Biophys.
325
139-143
1996
Luteovulum sphaeroides, Luteovulum sphaeroides f. sp. denitrificans
brenda
Adams, B.; Smith, A.T.; Bailey, S.; McEwan, A.G.; Bray, R.C.
Reactions of dimethylsulfoxide reductase from Rhodobacter capsulatus with dimethyl sulfide and with dimethyl sulfoxide: complexities revealed by conventional and stopped-flow spectrophotometry
Biochemistry
38
8501-8511
1999
Rhodobacter capsulatus
brenda
Bray, R.C.; Adams, B.; Smith, A.T.; Richards, R.L.; Lowe, D.J.; Bailey, S.
Reactions of dimethylsulfoxide reductase in the presence of dimethyl sulfide and the structure of the dimethyl sulfide-modified enzyme
Biochemistry
40
9810-9820
2001
Rhodobacter capsulatus (Q52675), Rhodobacter capsulatus
brenda
Cheng, V.W.; Rothery, R.A.; Bertero, M.G.; Strynadka, N.C.; Weiner, J.H.
Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase
Biochemistry
44
8068-8077
2005
Escherichia coli
brenda
Abo, M.; Tachibana, M.; Okubo, A.; Yamazaki, S.
Enantioselective deoxygenation of alkyl aryl sulfoxides by DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans
Bioorg. Med. Chem.
3
109-112
1995
Luteovulum sphaeroides, Luteovulum sphaeroides f.s. denitrificans
brenda
Miguel, L.; Meganthan, R.
Electron donors and the quinone involved in dimethyl sulfoxide reduction in Escherichia coli
Curr. Microbiol.
22
109-115
1991
Escherichia coli
-
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