Indian Journal of Chemistry Vol. 52A, Aug-Sept 2013, pp. 1019-1025 Synthetic glutathione peroxidase mimics: Effect of nucleophilicity of the aryl thiol cofactor on the antioxidant activity Krishna Pada Bhabak, Debasish Bhowmick & Govindasamy Mugesh* Department of Inorganic and Physical Chemistry, Indian Institute of Science, Bangalore, 560 012, India Email:
[email protected] Received 14 March 2013; accepted 30 April 2013 Catalytic activity of a series of potent amide- and amine-based organoselenium compounds are studied in the presence of various aromatic thiols having electron donating and electron withdrawing substituents on the phenyl ring. This study suggests that the antioxidant activities of the synthetic GPx mimics can be significantly increased by the incorporation of a suitable electron donating group on the phenyl ring of an aromatic thiol. Keywords: Glutathione peroxidase, Antioxidants, Organoselenium compounds, Aromatic thiols, Peroxide reduction, Thiols, Enzymatic activity, Enzyme mimics Glutathione peroxidase (GPx) is a selenocysteine with the reduction of peroxides. In presence of thiol containing mammalian antioxidant enzyme that cofactor such as GSH, the selenenic acid produces the catalyzes the reduction of harmful peroxides in the corresponding selenenyl sulfide intermediate presence of glutathione (GSH) as the thiol cofactor (E-SeSG). Nucleophilic attack of a second molecule and protects cells/biomolecules from oxidative of GSH at the Se-S bond regenerates the active site damage and inflammation.1 A catalytic mechanism with the release of GSH in its oxidized form (GSSG). has been proposed for the enzymatic activity that However, in the presence of a higher concentration of involves several redox reactions at the selenium peroxide such as in the condition of an ‘oxidative center of the active site selenocysteine residue.