Glutathione peroxidase and hydroperoxides: designing in silico approaches to case-studies

The mechanism of the oxidative step of glutathione peroxidases (GPx) has been well elucidated in silico and implies a long-range proton transfer mediated by a peroxide and a water molecule, followed by a nucleophilic attack to the peroxide O-O bond by the catalytic chalcogenolate. In this Thesis, we have revisited this enzymatic stage setting up a protocol to include dynamic effects of the protein environment and using a particular substrate, i.e. peroxynitrite, which might turn the activity of the endogenous peroxidatic system into a harmful hydrogen peroxide source.