EC Number   |
Cofactor |
Reference |
|---|
   1.8.5.3 | 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 |
713506 |
| 1.8.5.3 | 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 |
710991 |
| 1.8.5.3 | 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 |
675504 |
| 1.8.5.3 | 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 |
711196 |
| 1.8.5.3 | 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 |
712341 |
| 1.8.5.3 | menaquinone |
- |
763950 |
| 1.8.5.3 | methyl viologen |
- |
765088, 765095 |
| 1.8.5.3 | 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 |
711815 |
| 1.8.5.3 | 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 |
711885 |
| 1.8.5.3 | molybdenum cofactor |
- |
765770 |
