Designed histidine-rich peptide self-assembly for accelerating oxidase-catalyzed reactions

It is an important goal for supramolecular chemistry to develop synthetic enzyme mimics rivaling native enzymes, while de novo fabrication of such mimics remains a challenge. Alternatively, the catalytic groups from the supramolecular complex can be integrated with the active sites of natural enzymes. Herein, we present a supramolecular catalytic hybrid that is self-assembled from oligohistidine-based peptides and a heme-dependent peroxidase. The results indicate that the peptides altered the enzyme conformation, promoted the transitions between the resting and the intermediate states of the heme, and increased the turnover rate of the enzyme by up to three-fold. We propose that the histidine residues from the peptides may collaborate with the groups in the natural heme pocket to accelerate the catalytic cycles of the enzyme. Our observations underline the advantages of the supramolecular approach and suggest that molecular self-assembly may combine with enzymes to provide a simple strategy to engineer the enzymatic active sites.