Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis
Authorized Users Only
de Azambuja, Francisco
Article (Published version)
MetadataShow full item record
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 [Hf18O10(OH)26(SO4)13⋅(H2O)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.
Keywords:amino-acid-selective cleavage / artificial proteases / heterogeneous catalysis / metal-oxo clusters / protein hydrolysis
Source:Angewandte Chemie (International Edition), 2020, 59, 17, 1-9
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-172024)
- Serbian Academy of Sciences and Arts GA No. F-26.
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-810752)
- U.S. Department of Energy, Office of Basic Energy Sciences, Division of Material Sciences and Engineering, under award DE SC0010802.