Expanding the reactivity of inorganic clusters towards proteins: the interplay between the redox and hydrolytic activity of Ce(iv)-substituted polyoxometalates as artificial proteases.

ABSTRACT: The ability of soluble metal-oxo clusters to specifically interact with protein surfaces makes them attractive as potential inorganic drugs and as artificial enzymes. In particular, metal-substituted polyoxometalates (MS-POMs) are remarkably selective in hydrolyzing a range of different proteins. However, the influence of MS-POMs' redox chemistry on their proteolytic activity remains virtually unexplored. Herein we report a highly site-selective hydrolysis of hemoglobin (Hb), a large tetrameric globular protein, by a Ce(iv)-substituted Keggin polyoxometalate (Ce^IVK), and evaluate the effect of Ce^IVK's redox chemistry on its reactivity and selectivity as an artificial protease. At pH 5.0, incubation of Hb with Ce^IVK resulted in strictly selective protein hyd

SUBMITTER: Abdelhameed SAM 

PROVIDER: S-EPMC8356750 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature