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

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)-L-II and NHPI (N-hydroxyphthalimide) was developed. The (CuL)-L-II-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-I-radical intermediate species generated from the intramolecular redox process of (CuLH2)-L-II was critical for O-2 activation. Kinetic experiments showed that the activation of NHPI was the rate-determining step. Furthermore, activation of NHPI in the (CuL)-L-II-NHPI system was demonstrated by time-resolved EPR results. The persistent PINO (phthalimide-N-oxyl) radical mechanism for the aerobic oxidation of C-sp(3)-H bond was demonstrated.

Automated summary

In this study, a biomimetic approach for the aerobic oxidation of C-sp(3)-H bonds was developed, which showed excellent efficiency and mild reaction conditions. The Cu-I-radical intermediate species generated from the catalyst played a critical role in the reaction rate, and the PINO mechanism was demonstrated for the C-sp(3)-H bond oxidation.