Two‐Dimensional Tin Selenide (SnSe) Nanosheets Capable of Mimicking Key Dehydrogenases in Cellular Metabolism

• Published in: Angewandte Chemie International Edition Vol. 59; no. 9; pp. 3618 - 3623
• Main Authors: Gao, Meng, Wang, Zhenzhen, Zheng, Huizhen, Wang, Li, Xu, Shujuan, Liu, Xi, Li, Wei, Pan, Yanxia, Wang, Weili, Cai, Xiaoming, Wu, Ren'an, Gao, Xingfa, Li, Ruibin
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 24.02.2020
• Edition: International ed. in English
• Subjects: biocatalysts; Biomedical engineering; Biomimetic Materials - chemistry; Biomimetic Materials - metabolism; Catalysis; Catalytic activity; Chemical engineering; Dehydrogenases; density functional calculations; Ethanol; hydrogen evolution; Hydrogen-Ion Concentration; Metabolism; Mimicry; Nanosheets; Nanostructures - chemistry; nanozymes; Organic chemistry; Organic solvents; Oxidoreductases - chemistry; Oxidoreductases - metabolism; Selenide; Selenium - chemistry; structure–activity relationship; Temperature; Temperature tolerance; Thermodynamics; Tin - chemistry; Tin selenide; Tricarboxylic acid cycle; nanozymes; biocatalysts; density functional calculations; hydrogen evolution; structure-activity relationship
• ISSN: 1433-7851; 1521-3773
• DOI: 10.1002/anie.201913035

While dehydrogenases play crucial roles in tricarboxylic acid (TCA) cycle of cell metabolism, which are extensively explored for biomedical and chemical engineering uses, it is a big challenge to overcome the shortcomings (low stability and high costs) of recombinant dehydrogenases. Herein, it is shown that two‐dimensional (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 (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, this is the first report of a 2D SnSe nanozyme to mimic key dehydrogenases in cell metabolism. 2D SnSe is capable of mimicking native dehydrogenases to efficiently catalyze hydrogen transfer from 1‐(R)‐2‐(R′)‐ethanol groups. In contrast to susceptible native dehydrogenases, such as lactic dehydrogenase (LDH), SnSe is extremely tolerant to reaction condition changes (pH, temperature, and organic solvents) and displays extraordinary reusability.