Bound oxygen-atom transfer endows peroxidase-mimic M–N–C with high substrate selectivity

forming critically bound oxygen intermediates (M[double bond, length as m-dash]O) for oxygen-atom transfer and the consequent oxidization of substrates. Notably, owing to the embedded ligands in the rigid graphitic framework, surprisingly, the selectivity of M-N-C was even superior to that of commonly used horseradish peroxidase (HRP).