EC Number   |
|---|
    1.11.1.9 | - |
| 1.11.1.9 | computational kinetic modeling of selenol zwitterion anion as a glutathione peroxidase nanomimic. In the first step of the reaction, seleninic acid is produced through deprotonating of the selenol zwitterion anion in the presence of the hydrogen peroxide. Seleninic acid reacts with a thiol to form selenylsulfide in the second step. In the last step, selenylsulfide is reduced by the second thiol and regenerates selenolate anion through disulfide formation. The energy barrier of this reaction is 11.7 kcal per mol |
| 1.11.1.9 | crystal structure |
| 1.11.1.9 | hanging-drop vapour-diffusion method, 2.6 A resolution. The crystals are triclinic and belong to space group P1, with unit-cell parameters a = 38.187, b = 43.372, c = 56.870 A, alpha = 71.405, beta = 73.376, gamma = 89.633 |
| 1.11.1.9 | molecular docking study of interactions between 15 selenenylsulfide compounds that mimic glutathione peroxidase and the active site of glutathione reductase by molecular docking. The reduction of selenenylsulfide by glutathione reductase is important in GPx-like activity determination of GPx mimics |
| 1.11.1.9 | molecular modeling of mutant with all Cys residues changed to Ser |
| 1.11.1.9 | molecular modeling of the structure of seleno-hGPx2 |
| 1.11.1.9 | sitting drop vapor diffusion method, using 0.2 M LiSO4,0.2 M sodium acetate, 24% (w/v) PEG 8000, pH 4.5 for mutant enzyme U43C and 0.2 M NaH2PO4, 0.1 M MES, 32% (w/v) PEG-MME 5000, pH 6.0 for mutant enzyme U43S |
