EC Number   |
Metals/Ions |
Reference |
|---|
   1.8.5.3 | Molybdenum |
enzyme contains a molybdo-bis(pyranopterin guanine dinucleotide) cofactor |
724457 |
| 1.8.5.3 | 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 |
711193 |
| 1.8.5.3 | 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 |
711815 |
| 1.8.5.3 | Molybdenum |
reequired |
764899 |
| 1.8.5.3 | Molybdenum |
required |
764899, 765095, 765321, 765770 |
| 1.8.5.3 | Molybdenum |
required, Mo-DMSOR |
765088 |
| 1.8.5.3 | 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 |
675504 |
| 1.8.5.3 | 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) |
710783 |
| 1.8.5.3 | 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 |
713250 |
| 1.8.5.3 | 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 |
712155 |
