Computational Study Of Some Diselenide-Based Glutathione Peroxidase Mimics: Effect Of E Center Dot Center Dot Center Dot N (E = Se/Te) Intramolecular Interaction And E-E Bond Strength

There have been growing interests in studying small molecular weight organoselenium compounds as potential mimetics of glutathione peroxidase (GPx). In this regards, the intramolecular E center dot center dot center dot N (E = Se/Te) interactions and their effect on the E-E bond strengths in a series of diaryl dichalcogenides and their several derivatives have been investigated using density functional theory. The NBO, NBO deletion and AIM analyses suggest that the E center dot center dot center dot N interactions become stronger in polar solvent and correlate well with the E center dot center dot center dot N distances and E-E bond strengths. The calculated free energy changes of the different steps of the GPx-like catalytic cycle indicate that diselenides having stronger Se center dot center dot center dot N interactions have preference for the reverse GPx cycle, which is in agreement with the reported experimental observations.