Biomimetic synergistic effect of redox site and Lewis acid for construction of efficient artificial enzyme

In enzymatic catalysis, the redox site and Lewis acid are the two main roles played by metal to assist amino acids. However, the reported enzyme mimics only focus on the redox-active metal as redox site, while the redox-inert metal as Lewis acid has, to the best of our knowledge, not been studied, presenting a bottleneck of enzyme mimics construction. Based on this, a series of highly efficient M x V 2 O 5 ·nH 2 O peroxidase mimics with vanadium as redox site and alkaline-earth metal ion (M 2+ ) as Lewis acid are reported. Experimental results and theoretical calculations indicate the peroxidase-mimicking activity of M x V 2 O 5 ·nH 2 O show a periodic change with the Lewis acidity (ion potential) of M 2+ , revealing the mechanism of redox-inert M 2+ regulating electron transfer of V-O through non-covalent polarization and thus promoting H 2 O 2 adsorbate dissociation. The biomimetic synergetic effect of redox site and Lewis acid is expected to provide an inspiration for design of enzyme mimics.