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Discrete Hf18 Metal-oxo Cluster as a Heterogeneous Nanozyme for Site-Specific Proteolysis.
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2020-03-10 , DOI: 10.1002/anie.202001036
Jens Moons 1 , Francisco de Azambuja 1 , Jelena Mihailovic 2 , Karoly Kozma 3 , Katarina Smiljanic 2 , Mehran Amiri 3 , Tanja Cirkovic Velickovic 2, 4, 5, 6 , May Nyman 3 , Tatjana N Parac-Vogt 1
Affiliation  

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.

中文翻译:

离散的Hf18金属-氧簇作为特定位点蛋白水解的异质纳米酶。

通过非酶催化的蛋白质选择性水解是很难实现的,但是对于生物技术和蛋白质组学中的应用而言至关重要。在此,我们报道了以许多MOF中发现的相同六聚体基序为中心的离散ha金属-氧簇[Hf18 O10(OH)26(SO4)13⋅(H2 O)33](Hf18)用于在低缓冲液浓度下有效水解马心肌红蛋白(HHM)的催化剂。在HHM序列中存在的154个氨基酸中,仅在6个溶剂可及的天冬氨酸残基上观察到严格的选择性切割。机理实验表明,水解活性可能源自HfIV Lewis酸性位点和Hf18的Brønsted酸性表面的活化。X射线散射和ESI-MS表明,Hf18在这些条件下完全不溶,
更新日期:2020-03-10
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