Biomimetic catalytic aerobic oxidation of C-sp(3)-H bonds under mild conditions using galactose oxidase model compound CuL.

Developing highly efficient catalytic protocols for C-sp(3)-H bond aerobic oxidation under mild conditions is a long-desired goal of chemists. Inspired by nature, a biomimetic approach for the aerobic oxidation of C-sp(3)-H by galactose oxidase model compound CuL and NHPI (-hydroxyphthalimide) was developed. The CuL-NHPI system exhibited excellent performance in the oxidation of C-sp(3)-H bonds to ketones, especially for light alkanes. The biomimetic catalytic protocol had a broad substrate scope. Mechanistic studies revealed that the Cu-radical intermediate species generated from the intramolecular redox process of CuLH was critical for O activation. Kinetic experiments showed that the activation of NHPI was the rate-determining step. Furthermore, activation of NHPI in the CuL-NHPI system was demonstrated by time-resolved EPR results. The persistent PINO (phthalimide--oxyl) radical mechanism for the aerobic oxidation of C-sp(3)-H bond was demonstrated.