Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 23, Pages 9094-9101Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202001036
Keywords
amino-acid-selective cleavage; artificial proteases; heterogeneous catalysis; metal-oxo clusters; protein hydrolysis
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Funding
- KU Leuven
- Research Foundation Flanders (FWO)
- Ministry of Education, Science and Technological Development of the Republic of Serbia [OI172024]
- Serbian Academy of Sciences and Arts [F-26]
- European Commission, under the Horizon 2020, FoodEnTwin project [810752]
- U.S. Department of Energy, Office of Basic Energy Sciences, Division of Material Sciences and Engineering [DE SC0010802]
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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)] (Hf-18), 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 Hf-IV Lewis acidic sites and the Bronsted acidic surface of Hf-18. X-ray scattering and ESI-MS revealed that Hf-18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf-18 cluster, and not from smaller, soluble Hf species that could leach into solution.
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