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

ABSTRACT: Advances in nanoscience have stimulated the wide exploration of nanozymes as alternatives to enzymes. Nonetheless, nanozymes often catalyze multiple reactions and are not specialized to a specific substrate, restricting their broad application. Here, we report that the substrate selectivity of the peroxidase-mimic M-N-C can be significantly altered via forming bound intermediates with variable interactions with substrates according to the type of metal. Taking two essential reactions in chemical sensing as an example, Fe-N-C and Co-N-C showed opposite catalytic selectivity for the oxidation of 3,3',5,5'-tetramethylbenzidine (TMB) and 3-aminophthalhydrazide (luminol), respectively, by factors of up to 200-fold. It was revealed that specific transition metal-N coordination was the origin of the selective activation of H₂O₂ 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).

SUBMITTER: Chen X

PROVIDER: S-EPMC8246298 | biostudies-literature |

REPOSITORIES: biostudies-literature

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