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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
- tord
- narghi
- frdabcd
-
mo-containing
-
bismolybdopterin
- wiv
- menaquinol
The enzyme appears in viruses and cellular organisms
Synonyms
dimethyl sulfoxide/trimethylamine N-oxide reductase, dimethylsulfoxide reductase, DmsA, DmsABC, DmsC, DMSO reductase, DMSOR, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DmsABC
DMSO reductase
DMSOR
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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
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PATHWAY SOURCE
PATHWAYS
KEGG
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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-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
-
-
?
(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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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
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdenum cofactor
-
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
[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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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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
Molybdenum
-
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
-
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
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
-
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
-
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
Molybdenum
-
the complex trichloro(2',5'-quinoid-7,8-dihydro-(2'H+,6H)-pterin)oxomolybdenum(IV) is able to reduce the substrate dimethyl sulfoxide to dimethyl sulfide under very mild conditions and accompanied by oxidation of the quinoid dihydropterin to pterin and oxidation of Mo(IV) to Mo(VI)
Tungsten
may replace molybdenum. Tungsten is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of dimethylsulfoxide but shows no significant ability to catalyse the oxidation of dimethylsulfide
Tungsten
-
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 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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-n-heptyl-4-hydroxyquinoline N-oxide
-
residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the binding of the MQH2 inhibitor analogue 2-n-heptyl-4-hydroxyquinoline N-oxide
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
menaquinol analogue. 2-n-Heptyl-4-hydroxyquinoline-N-oxide fluorescence is quenched when 2-n-heptyl-4-hydroxyquinoline-N-oxide binds to the holoenzyme DmsABC. The binding stoichiometry is about 1:1. There is one high-affinity 2-n-heptyl-4-hydroxyquinoline-N-oxide binding site per DmsABC molecule located in the DmsC subunit. The interaction follows a two-step equilibrium model, a fast bimolecular step followed by a slow unimolecular step. The quenching of 2-n-heptyl-4-hydroxyquinoline-N-oxide fluorescence occurs in the bimolecular step
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
0.33
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
0.095
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
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.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
-
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
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
mutant DELTAN21, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
0.14
mutant V20Y/DELTAN21/P27G, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
0.33
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
125
mutant R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
141
wild-type, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
2.63
mutant R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
5.22
mutant V20Y/DELTAN21/P27G, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
5.91
mutant DELTAN21, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
7.72
wild-type, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
7.97
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
overexpression of membrane anchor subunit DmsC tagged with a dystrophin-specific amino acid sequence in COS-1 or Mc-RH777 cells, results in localization to endoplasmic reticulum
brenda
-
membrane-intrinsic subunit DmsC 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
brenda
-
the terminal reductase and the dehyrogenases linking the various electron donors to the electron transport chain are membrane bound
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
anaerobic growth on sulfoxides is solely due to DmsABC expression
physiological function
-
deletion mutant of catayltic subunit DmsA is attenuated in acute disease in an aerosol infection model
physiological function
-
deletion mutants lacking dimethysulfoxide reductase retain the ability to use trimethylamine N-oxide as an electron acceptor and the trimethylamine N-oxid reductase activity is unaltered
physiological function
-
more than 50% of chlorate-resistant mutants isolated are defective in the biosynthesis of the molybdenum cofactor and all of these mutants accumulate the precursor form of the enzyme. About 45% of the mutants contain the same level of molybdenum cofactor as the parent strain and exhibit normal levels of DMSO reductase and nitrate reductase activities when chlorate is absent from the medium, but the activities of these enzymes are depressed when chlorate is present. Much of the accumulated precursor form of the enzyme in a molybdenum cofactor-deficient mutant is bound to the cytoplasmic membrane and is sensitive to treatment with proteinase K from the periplasmic side of the membrane. Results suggest that 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
physiological function
-
mutants of Escherichia coli blocked in menaquinone biosynthesis, menB, menC, and menD, are unable to grow with DMSO as an electron acceptor, even though the terminal reductase is present in these mutants. Both growth and DMSO reduction can be restored in these mutants by growth in the presence of the menaquinone intermediates, o-succinylbenzoate and 1,4-dihydroxy-2-naphthoate, depending on the metabolic block of the mutant
physiological function
Luteovulum sphaeroides f. sp. denitrificans
-
more than 50% of chlorate-resistant mutants isolated are defective in the biosynthesis of the molybdenum cofactor and all of these mutants accumulate the precursor form of the enzyme. About 45% of the mutants contain the same level of molybdenum cofactor as the parent strain and exhibit normal levels of DMSO reductase and nitrate reductase activities when chlorate is absent from the medium, but the activities of these enzymes are depressed when chlorate is present. Much of the accumulated precursor form of the enzyme in a molybdenum cofactor-deficient mutant is bound to the cytoplasmic membrane and is sensitive to treatment with proteinase K from the periplasmic side of the membrane. Results suggest that 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
physiological function
-
deletion mutant of catayltic subunit DmsA is attenuated in acute disease in an aerosol infection model
Show AA Sequence and Transmembrane Helices (2410 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the DmsAB dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Results suggest that the membrane-intrinsic subunit DmsC 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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
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
proteolytic modification
Luteovulum sphaeroides f. sp. denitrificans
-
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray absorption spectroscopic analysis of the molybdenum active site of Escherichia coli dimethyl sulfoxide reductase contained within its native membranes.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
-
oxidized Mo(VI)-form, to 3.5 A resolution. 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
-
x-ray absorption spectroscopy study. Dimethyl sulfoxide reductase reduced with trimethylarsine is structurally analogous to the physiologically relevant dimethyl sulfide reduced dimethyl suldfoxide reductase. These species should be regarded as formal MoIV species with a classical coordination complex of trimethylarsine oxide, with no special structural distortions. The similarity of the trimethylarsine and dimethyl sulfide complexes suggests that the dimethyl sulfide reduced enzyme possesses a classical coordination of DMSO with no special elongation of the S-O bond
-
damaged enzyme form derived from an intermediate formed by reaction of DMSOR with dimethylsulfide and reaction with oxygen, to 2.0 A resolution. All four thiolate ligands and Ogamma of serine-147 remain coordinated to molybdenum, there are no terminal oxygen ligands and molybdenum is Mo(VI)
protein with tungsten in place of molybdenum, to 2.0 A resolution
to 1.88 A resolution, space group P41212. Spherical protein, consists of four domains with a funnel-like cavity that leads to the freely accessible metal-ion redox center. The bis(molybdopterin guanine dinucleotide) molybdenum 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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A178Q
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/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/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
G167N
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/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
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/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H85T/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
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/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Q179I
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
R217Q
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)
T148S
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/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
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/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
additional information
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulated under anaerobic conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
brenda
McNamara, J.; Hillier, I.; Bhachu, T.; Garner, C.
The nature and function of the catalytic centres of the DMSO reductases
Dalton Trans.
2005
3572-3579
2005
synthetic construct
-
brenda
Solomon, P.S.; Lane, I.; Hanson, G.R.; McEwan, A.G.
Characterisation of the pterin molybdenum cofactor in dimethylsulfoxide reductase of Rhodobacter capsulatus
Eur. J. Biochem.
246
200-203
1997
Rhodobacter capsulatus
brenda
Simala-Grant, J.L.; Weiner, J.H.
Modulation of the substrate specificity of Escherichia coli dimethylsulfoxide reductase
Eur. J. Biochem.
251
510-515
1998
Escherichia coli
brenda
Ridge, J.P.; Aguey-Zinsou, K.F.; Bernhardt, P.V.; Hanson, G.R.; McEwan, A.G.
The critical role of tryptophan-116 in the catalytic cycle of dimethylsulfoxide reductase from Rhodobacter capsulatus
FEBS Lett.
563
197-202
2004
Rhodobacter capsulatus
brenda
Daruwala, R.; Meganathan, R.
Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli
FEMS Microbiol. Lett.
83
255-259
1991
Escherichia coli
brenda
Baltes, N.; Hennig-Pauka, I.; Jacobsen, I.; Gruber, A.; Gerlach, G.
Identification of dimethyl sulfoxide reductase in Actinobacillus pleuropneumoniae and its role in infection
Infect. Immun.
71
6784-6792
2003
Actinobacillus pleuropneumoniae, Actinobacillus pleuropneumoniae serotype 7
brenda
George, G.; Doonan, C.; Rothery, R.; Boroumand, N.; Weiner, J.
X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase
Inorg. Chem.
46
2-4
2007
Escherichia coli
brenda
George, G.; Nelson, K.; Harris, H.; Doonan, C.; Rajagopalan, K.
Interaction of product analogues with the active site of Rhodobacter sphaeroides dimethyl sulfoxide reductase
Inorg. Chem.
46
3097-3104
2007
Luteovulum sphaeroides
brenda
Sambasivarao, D.; Weiner, J.
Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation
J. Bacteriol.
173
5935-5943
1991
Escherichia coli
brenda
Zhao, Z.; Weiner, J.
Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli
J. Biol. Chem.
273
20758-20763
1998
Escherichia coli
brenda
Rothery, R.A.; Trieber, C.A.; Weiner, J.H.
Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase
J. Biol. Chem.
274
13002-13009
1999
Escherichia coli
brenda
Johnson, K.; Rajagopalan, K.
An active site tyrosine influences the ability of the dimethyl sulfoxide reductase family of molybdopterin enzymes to reduce S-oxides
J. Biol. Chem.
276
13178-13185
2001
Luteovulum sphaeroides
brenda
Stewart, L.J.; Bailey, S.; Bennett, B.; Charnock, J.M.; Garner, C.D.; McAlpine, A.S.
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site
J. Mol. Biol.
299
593-600
2000
Rhodobacter capsulatus (Q52675), Rhodobacter capsulatus
brenda
Simala-Grant, J.; Weiner, J.
Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
Microbiology
142
3231-3239
1996
Escherichia coli
brenda
Hanlon, S.; Graham, D.; Hogan, P.; Holt, R.; Reeve, C.; Shaw, A.; McEwan, A.
Asymmetric reduction of racemic sulfoxides by dimethyl sulfoxide reductases from Rhodobacter capsulatus, Escherichia coli and Proteus species
Microbiology
144
2247-2253
1998
Escherichia coli, Proteus mirabilis, Rhodobacter capsulatus
brenda
Masui, H.; Fukase, Y.; Satoh, T.
Accumulation on the cytoplasmic membrane of the precursor to dimethyl sulfoxide reductase in molybdenum cofactor-deficient mutants of Rhodobacter sphaeroides f. sp. denitrificans
Plant Cell Physiol.
33
463-469
1992
Luteovulum sphaeroides, Luteovulum sphaeroides f. sp. denitrificans
-
brenda
Turner, R.; Busaan, J.; Lee, J.; Michalak, M.; Weiner, J.
Expression and epitope tagging of the membrane anchor subunit (DmsC) of Escherichia coli dimethyl sulfoxide reductase
Protein Eng.
10
285-290
1997
Escherichia coli
brenda
Schindelin, H.; Kisker, C.; Hilton, J.; Rajagopalan, K.; Rees, D.
Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
Science
272
1615-1621
1996
Luteovulum sphaeroides
brenda
Tang, H.; Rothery, R.A.; Weiner, J.H.
A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase
Biochim. Biophys. Acta
1827
730-737
2013
Escherichia coli (P18775), Escherichia coli
brenda
Hernandez-Marin, E.; Ziegler, T.
A kinetic study of dimethyl sulfoxide reductase based on density functional theory
Can. J. Chem.
88
683-693
2010
Rhodobacter capsulatus (Q52675)
-
brenda
Tang, H.; Rothery, R.A.; Voss, J.E.; Weiner, J.H.
Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion
J. Biol. Chem.
286
15147-15154
2011
Escherichia coli (P18775)
brenda
Li, J.; Mata, R.; Ryde, U.
Large density-functional and basis-set effects for the DMSO reductase catalyzed oxo-transfer reaction
J. Chem. Theory Comput.
9
1799-1807
2013
Rhodobacter capsulatus (Q52675)
brenda
Ha, Y.; Tenderholt, A.L.; Holm, R.H.; Hedman, B.; Hodgson, K.O.; Solomon, E.I.
Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on monooxo Mo(IV) and bisoxo Mo(VI) bis-dithiolenes insights into the mechanism of oxo transfer in sulfite oxidase and its relation to the mechanism of DMSO reductase
J. Am. Chem. Soc.
136
9094-9105
2014
Escherichia coli (P18775)
brenda
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