The isolation and crystal structure of a cyclic selenenate ester derived from bis(2,6-diformyl-4-tert-butylphenyl)diselenide and its glutathione peroxidase-like activity

Abstract

Enzyme mimicry: Halogenation of diselenide 1 affords the cyclic selenenate ester 2 (see scheme) through a highly unstable selenenic acid intermediate. Compound 2 exhibits a strong intramolecular nonbonding Se···O interaction. Both 1 and 2 show excellent glutathione peroxidase-like catalytic activity

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