Nonheme Diiron Oxygenase Mimic That Generates a Diferric-Peroxo Intermediate Capable of Catalytic Olefin Epoxidation and Alkane Hydroxylation Including Cyclohexane.

Herein are described substrate oxidations with H 2 O 2 catalyzed by [Fe II (IndH)(CH 3 CN) 3 ](ClO 4 ) 2 [IndH = 1,3-bis(2'-pyridylimino)isoindoline], involving a spectroscopically characterized (μ-oxo)(μ-1,2-peroxo)diiron(III) intermediate ( 2 ) that is capable of olefin epoxidation and alkane hydroxylation including cyclohexane. Species 2 also converts ketones to lactones with a decay rate dependent on [ketone], suggesting direct nucleophilic attack of the substrate carbonyl group by the peroxo species. In contrast, peroxo decay is unaffected by the addition of olefins or alkanes, but the label from H 2 18 O is incorporated into the the epoxide and alcohol products, implicating a high-valent iron-oxo oxidant that derives from O-O bond cleavage of the peroxo intermediate. These results demonstrate an ambiphilic diferric-peroxo intermediate that mimics the range of oxidative reactivities associated with O 2 -activating nonheme diiron enzymes.