Discrete Hf18 Metal-oxo Cluster as a Heterogeneous Nanozyme for Site-Specific Proteolysis.

Angewandte Chemie
Jens MoonsTatjana N Parac-Vogt

Abstract

The selective hydrolysis of proteins by non-enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal-oxo cluster [Hf18 O10 (OH)26 (SO4 )13 ⋅(H2 O)33 ] (Hf18 ), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18 . X-ray scattering and ESI-MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.

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Citations

Aug 6, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Laura S Van RompuyTatjana N Parac-Vogt
Feb 6, 2021·Analytical Methods : Advancing Methods and Applications·Huifei ZhongRui Zhao
Feb 19, 2021·Accounts of Chemical Research·Francisco de AzambujaTatjana N Parac-Vogt

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