EC Number   |
Reaction  |
Reference |
|---|
   1.8.5.3 | dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol |
- |
- |
| 1.8.5.3 | 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 |
724687 |
| 1.8.5.3 | 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 |
725605 |
| 1.8.5.3 | 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 |
765321 |
| 1.8.5.3 | 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 |
765321 |
