1.8.5.3: respiratory dimethylsulfoxide reductase
This is an abbreviated version!
For detailed information about respiratory dimethylsulfoxide reductase, go to the full flat file.
Word Map on EC 1.8.5.3
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1.8.5.3
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rhodobacter
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sphaeroides
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molybdoenzyme
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molybdopterin
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capsulatus
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dithiolene
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pyranopterins
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narghi
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tord
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bismolybdopterin
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mo-containing
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high-g
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menaquinol
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wiv
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frdabcd
- 1.8.5.3
- rhodobacter
- sphaeroides
-
molybdoenzyme
- molybdopterin
- capsulatus
-
dithiolene
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pyranopterins
- narghi
- tord
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bismolybdopterin
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mo-containing
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high-g
- menaquinol
- wiv
- frdabcd
Reaction
Synonyms
dimethyl sulfoxid reductase, dimethyl sulfoxide reductase, dimethyl sulfoxide/trimethylamine N-oxide reductase, dimethyl sulfoxie reductase, dimethylsulfoxide reductase, dms, DmsA, DmsABC, DmsABC sulfoxide reductase, DmsC, DMSO reductase, DMSOR, dorA, More, respiratory dimethyl sulfoxide reductase
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Metals Ions
Metals Ions on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase
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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
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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
Molybdenum
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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)
W-DMSOR, can substitute for molybdenum, the W-DMSOR shows 30fold higher activity than the molybdenum-containing enzyme, Mo-DMSOR. Rapid-scanning stopped-flow traces showing the enzyme monitored turnover of 0.032 mM W-DMSOR with 10 mM sodium dithionite and 0.25 mM DMSO performed in 50 mM KH2PO4, 0.6 mM EDTA, pH 6.0 at 25°C
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
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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 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
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. At the end of turnover, in the presence of excess dithionite, the fully reduced W-DMSOR accumulates. That no W(IV)-DMSO intermediate is seen during turnover indicates that DMS does not rebind to the oxidized W-DMSOR
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. At the end of turnover, in the presence of excess dithionite, the fully reduced W-DMSOR accumulates. That no W(IV)-DMSO intermediate is seen during turnover indicates that DMS does not rebind to the oxidized W-DMSOR