Cover Feature: Cleavage of a Peroxide Bond <i>via</i> a Dual Attack by Functional Mimics of Glutathione Peroxidase (Chem. Eur. J. 16/2025)

Non-metal-containing peroxidases, including glutathione peroxidase (GPx), peroxiredoxins, peroxide sensor protein OxyR, and Populus trichocarpa GPX5 control cellular redox levels by catalytically reducing H2O2. The remarkably higher reactivity of the enzyme as compared to the fully dissociated synthetic selenolate or thiolate molecule is probably due to a dual attack on the peroxide bond (O−O) by the enzyme. In their Research Article (DOI: 10.1002/chem.202403483), G. Roy and co-workers report the cleavage of O−O bond of H2O2 via a dual attack by synthetic model compounds similar to the non-metal-containing peroxidase enzymes.