Expanding the reactivity of inorganic clusters towards proteins: the interplay between the redox and hydrolytic activity of Ce(<scp>iv</scp>)-substituted polyoxometalates as artificial proteases
Shorok A. M. Abdelhameed, Hong Giang T. Ly, Jens Moons, Francisco de Azambuja, Paul Proost, Tatjana N. Parac‐Vogt
Abstract
K form in the presence of protein at pH 7.4. In agreement with these results, careful mapping of all hydrolyzed Asp-X bonds on the protein structure revealed that the lower reactivity toward the α-chain was consistent with the presence of more redox-active amino acids (Tyr and His) in this subunit in comparison with the β-chain. This points towards a link between the presence of the redox-active sites on the protein surface and efficiency and selectivity of redox-active MS-POMs as artificial proteases. More importantly, the study provides a way to tune the redox and hydrolytic reactivity of MS-POMs towards proteins through adjustment of reaction parameters like temperature and pH.