Author(s) Gao, M.; Wang, Z.; Zheng, H.; Wang, L.; Xu, S.; Liu, X.; Li, W.; Pan, Y.; Wang, W.; Cai, X.; Wu, R.; Gao, X.; Li, R.
Journal Angew Chem Int Ed Engl
Date Published 2019 Dec 11

While dehydrogenases play crucial roles in tricarboxylic acid (TCA) cycle of cell metabolism, which are extensively explored for biomedical and chemical engineering uses, it's a big challenge to overcome the shortcomings (low stability and high costs) of recombinant dehydrogenases. Herein, we made an interesting finding that two-dimension (2D) SnSe is capable of mimicking native dehydrogenases to efficiently catalyze hydrogen transfer from 1-(R)-2-(R')-ethanol groups. In contrary to susceptible native dehydrogenases, lactic dehydrogenase (LDH) for instance, SnSe is extremely tolerant to reaction condition changes ( e.g. pH, temperature and organic solvents) and displays extraordinary reusable capability. Structure-activity analysis indicates that the single-atom structure, Sn vacancy and hydrogen binding affinity of SnSe may be responsible for their catalytic activity. Overall, our findings define the first report of a 2D SnSe nanozyme to mimic key dehydrogenases in cell metabolism.

DOI 10.1002/anie.201913035
ISSN 1521-3773
Citation Angew Chem Int Ed Engl. 2019.

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