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

Proteolysis
DOI: 10.1002/anie.202001036 Publication Date: 2020-03-10T10:41:30Z
ABSTRACT
The selective hydrolysis of proteins by non-enzymatic catalysis is difficult to achieve, yet it 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 centred the same hexamer motif found many MOFs, acts as a heterogeneous catalyst efficient horse heart myoglobin (HHM) low buffer concentrations. Among 154 amino acids present sequence HHM, strictly cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest hydrolytic activity likely derived from actuation HfIV Lewis acidic sites Brønsted surface Hf18 . X-ray scattering ESI-MS revealed completely insoluble these conditions, confirming HHM caused reaction solid cluster, not smaller, soluble Hf species could leach into solution.
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