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Information on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase
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1.8.5.3 respiratory dimethylsulfoxide reductaseIUBMB Comments
The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron-sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. The electrons are passed through DmsB to DmsA and on to DMSO. The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
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Word Map
- 1.8.5.3
- rhodobacter
- sphaeroides
-
molybdoenzyme
- molybdopterin
- capsulatus
-
dithiolene
-
pyranopterins
- narghi
- tord
-
bismolybdopterin
-
mo-containing
-
high-g
- menaquinol
- wiv
- frdabcd
The enzyme appears in viruses and cellular organisms
Synonyms
dmso reductase, dimethyl sulfoxide reductase, dmsor, dmsabc, dimethylsulfoxide reductase, dimethyl sulfoxide/trimethylamine n-oxide reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimethyl sulfoxide reductase
dimethylsulfoxide reductase
-
-
-
-
dms
DmsA
DmsABC
DmsABC sulfoxide reductase
DMSO reductase
DMSOR
DMSO reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
-
-
-
-
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
according to density functional theory, the reaction between dimethyl sulfoxide and the model complex [Mo(OPh)(C2S2H2)2]- proceeds in one associative step. In the optimized transition state, the bond between the metal and dimethyl sulfoxide is being formed through the oxygen atom of dimethyl sulfoxide while the S-O bond in the substrate is weakening
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
computational studies show that the enzyme follows a two-step associative mechanism with the binding of dimethylsulfoxide in the first step and the oxygen-atom transfer and dissociation of the dimethylsulfide product in the second step. The first transition state is close in energy to the intermediate (within about 10 kJ/mol), whereas the rate-limiting barrier is observed for the second step
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
reaction mechanism, overview. Reactions of reduced enzyme with DMSO are biphasic in the pH 6-10 range, and reveal a fast initial substrate binding phase followed by a catalytic phase that is independent of the substrate concentration. Spectral deconvolution of the absorption spectrum over the time course of the reaction reveals contributions from four distinct species that are catalytically relevant. These include an oxidized Mo(VI) state, a one-electron reduced Mo(V) high-g split intermediate, fully reduced enzyme in the Mo(IV) state, and a reduced enzyme form with DMSO bound to the Mo site. The distorted trigonal prismatic active site structure in DMSO reductase imparts significant electronic structure contributions to enzymatic catalysis
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
reaction mechanism, overview. The distorted trigonal prismatic active site structure in DMSO reductase imparts significant electronic structure contributions to enzymatic catalysis
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SYSTEMATIC NAME
IUBMB Comments
dimethyl sulfide:menaquinone oxidoreductase
The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron-sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. The electrons are passed through DmsB to DmsA and on to DMSO. The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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-naphthoquinol
dimethylsulfide + H2O + 2,3-dimethyl-1,4-naphthoquinone
-
-
-
-
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
-
-
?
(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
Cereibacter 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
Cereibacter 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
Cereibacter 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
Cereibacter 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 + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + methyl viologen
dimethylsulfide + oxidized methyl viologen + H2O
-
-
-
?
dimethylsulfoxide + methyl viologen
dimethylsulfide + oxidized methyl viologen + H2O
-
activity of mutant C176D of periplasmic nitrate reductase NapA (EC 1.9.6.1), no activity with wild-type NapA or C176S/A NapA mutants
-
-
?
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
r
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
r
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
additional information
?
-
-
for all substrates studied, enzyme catalyzes deoxygenation of (S)-sulfoxides predominantly
-
-
?
additional information
?
-
Cereibacter 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
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
-
CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome, serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE and DmsF-independent manner
-
-
-
additional information
?
-
-
CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome, serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE and DmsF-independent manner
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylsulfide + menaquinone + H2O
dimethylsulfoxide + menaquinol
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
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dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
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dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
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dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
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dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[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
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
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presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
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protein contains 1 mol of molybdenum, 4 mol of organic phosphate, and 2 mol of guanine per mole of protein
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
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the bis-molybdopterin guanine dinucleotide cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center
Fe-S center
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residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the transfer of electrons from MQH2 to iron-sulfur cluster FS4
Fe-S center
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significant spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the Mo-bisMGD of subunit DmsA. This interaction is significantly modified in a DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA
molybdenum bis-molybdopterin guanine dinucleotide
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reaction profile for oxygen atom transfer from dimethylsulfoxide to [Mo(IV)(OMe)(S2C2H2)2]1- compared to the corresponding reaction with [W(IV)(OMe)(S2C2H2)2]1-. Both reaction profiles involve two transition states separated by a well-defined intermediate. The second transition state TS2 is clearly rate-limiting for the Mo system, and the two transition states have a similar energy for the W system. The activation energy for oxygen atom transfer from dimethylsulfoxide to [W(IV)(OMe)(S2C2H2)2]1- is ca. 23 kJ per mol lower for the corresponding reaction with Mo, consistent with the significantly faster rate of reduction of dimethylsulfoxide by Rhodobacter capsulatus W-dimethylsulfoxide reductase than by its Mo counterpart. The geometrical constraints imposed by the protein on the metal centre of the Mo- and W-dimethylsulfoxide reductases facilitate oxygen atom transfer by favouring a trigonal prismatic geometry for the transition state TS2 that is close to that observed for the metal in the oxidised form of each of these enzymes. The major effect of different tautomers of a simplified form of the pyran ring-opened, dihydropterin state, a significant lowering of the activation barrier associated with TS2, is observed for a protonated form of a tautomer that involves conjugation between the pyrazine and metallodithiolene rings
molybdenum bis-molybdopterin guanine dinucleotide
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the molybdenum cofactor in dimethylsulfoxide reductase is bis(molybdopterin guanine dinucleotide) molybdenum. Protein contains 1 mol Mo and 2 mol GMP. Approximately 2 mol. electrons/2 mol molybdopterin guanine dinucleotide reduce 2,6-dichloroindophenol. Presence of one molybdopterin guanine dinucleotide moiety with a pyrazine ring at the oxidation level of a dihydropteridine and one molybdopterin guanine dinucleotide moiety with a pyrazine ring at the oxidation level of a fully aromatic pteridine
molybdenum cofactor
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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. W116 plays a critical role in stabilizing the hexacoordinate monooxo MoVI form of the enzyme and prevents the formation of a dioxo pentacoordinate MoVI species
molybdenum cofactor
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MoCo, the cofactor coordinates organic molybdopterin to molybdenum, over 50 different molybdopterin enzymes are known to catalyze a variety of chemistries in the cycling of C, N, S, As, and Se, all relying on the same basic cofactor, the MoCo. Kinetic consequences of the exchange of the endogenous ligand to molybdenum with other ligands within the cofactor of DMSO reductase family enzymes, overview. The mutant C176D of periplasmic nitrate reductase NapA (EC 1.9.6.1) is active with DMSO (and artificial cosubstrate methyl viologen), while the wild-type NapA is not
molybdenum cofactor
pterin-based cofactor MoCo, molybdenum is not active in cells until it forms the MoCo. The DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzyme DmsA is a type III enzyme
molybdenum cofactor
pterin-based cofactor MoCo, molybdenum is not active in cells until it forms the MoCo. The DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzyme DmsA is a type III enzyme. The Mo amino acid ligand in the MoCo of Halobacterium salinarum DmsA is an aspartate residue in all halophilic archaea instead of a serine residue
molybdenum cofactor
pterin-based cofactor MoCo, the unique cofactor contains the ligand pyranopterin ene-1,2-dithiolate. Mechanism for mature Moco formation, overview. Bacterial DMSO reductase family enzymes possess a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor that is obtained by adding GMP to the MPT terminal phosphates. Enzymes that belong to the DMSO reductase enzyme family possess two coordinated MPTs, with one of the MPTs adopting an SO family configuration and the other a more distorted XO enzyme family structure, role of MPT in catalysis
molybdenum cofactor
pterin-based cofactor MoCo, the unique cofactor contains the ligand pyranopterin ene-1,2-dithiolate. Mechanism for mature Moco formation, overview. Bacterial DMSO reductase family enzymes possess a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor that is obtained by adding GMP to the MPT terminal phosphates. Enzymes that belong to the DMSO reductase enzyme family possess two coordinated MPTs, with one of the MPTs adopting an SO family configuration and the other a more distorted XO enzyme family structure, role of MPT in catalysis
molybdenum cofactor
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
molybdenum cofactor
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
additional information
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CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. In-frame deletion mutagenesis of dmsE (swp3461) and analysis
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additional information
kinetic and spectroscopic analysis of molybdenum-DMSO reductase and a tungsten-substituted form of DMSO reductase, overview. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called high-g split type that exhibits markedly greater g-anisotropy than the corresponding Mo(V) signal of the native form of the enzyme, with the g values shifted to higher magnetic field by as much as DELTAgave = 0.056. Deuteration of the enzyme confirms that the coupled proton is solvent-exchangeable, allowing to accurately simulate the tungsten hyperfine coupling. Global curve-fitting analysis of UV/vis absorption spectra observed in the course of the reaction of the tungsten-substituted enzyme with sodium dithionite affords a well-defined absorption spectrum for the W(V) species. The absorption spectrum for this species exhibits significantly larger molar extinction coefficients than either the reduced or the oxidized spectrum. This spectrum, in conjunction with those for fully oxidized W(VI) and fully reduced W(IV) enzyme, is used to deconvolute the absorption spectra seen in the course of turnover, in which the enzyme is reacted with sodium dithionite and DMSO, demonstrating that the W(V) is an authentic catalytic intermediate that accumulates to approximately 50% of the total enzyme in the steady state
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additional information
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kinetic and spectroscopic analysis of molybdenum-DMSO reductase and a tungsten-substituted form of DMSO reductase, overview. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called high-g split type that exhibits markedly greater g-anisotropy than the corresponding Mo(V) signal of the native form of the enzyme, with the g values shifted to higher magnetic field by as much as DELTAgave = 0.056. Deuteration of the enzyme confirms that the coupled proton is solvent-exchangeable, allowing to accurately simulate the tungsten hyperfine coupling. Global curve-fitting analysis of UV/vis absorption spectra observed in the course of the reaction of the tungsten-substituted enzyme with sodium dithionite affords a well-defined absorption spectrum for the W(V) species. The absorption spectrum for this species exhibits significantly larger molar extinction coefficients than either the reduced or the oxidized spectrum. This spectrum, in conjunction with those for fully oxidized W(VI) and fully reduced W(IV) enzyme, is used to deconvolute the absorption spectra seen in the course of turnover, in which the enzyme is reacted with sodium dithionite and DMSO, demonstrating that the W(V) is an authentic catalytic intermediate that accumulates to approximately 50% of the total enzyme in the steady state
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additional information
tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases
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additional information
tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Molybdenum
tungstate
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
Tungsten
additional information
Molybdenum
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the molybdenum cofactor is necessary for proteolytic processing of the precursor to the mature enzyme on the periplasmic side of the membrane, whereas binding of the precursor to the membrane and translocation across it can occur in the absence of the cofactor
Molybdenum
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the oxidized active site has four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. The oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. Results suggest that the form found in vivo is the monooxobis(molybdopterin) species
Molybdenum
enzyme contains a molybdo-bis(pyranopterin guanine dinucleotide) cofactor
Molybdenum
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
Molybdenum
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the bis-molybdopterin guanine dinucleotide cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center
Molybdenum