化学
柠檬酸循环
酶
催化作用
新陈代谢
三羧酸
脱氢酶
醇脱氢酶
生物化学
NAD+激酶
硒化物
组合化学
锡
有机化学
硒
作者
Meng Gao,Zhenzhen Wang,Huizhen Zheng,Li Wang,Shujuan Xu,Xi Liu,Wei Li,Yanxia Pan,Weili Wang,Xiaoming Cai,Ren’an Wu,Xingfa Gao,Ruibin Li
标识
DOI:10.1002/anie.201913035
摘要
Abstract 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.
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