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Important Progress in Rational Design of Single-atom Nanozyme

Updated: 2021-05-10

On May 6, a research article entitled Matching the Kinetics of Native Enzymes with a Single-atom Iron Nanozyme was published in Nature Catalysis. In this paper, a FeN3P-centered single-atom nanozyme (FeN3P-SAzyme) is designed, which controls the electronic structure of the active site of single-atom iron through the precise coordination of phosphorus and nitrogen, and that shows catalytic activity and kinetics similar to that of natural enzyme. In particular, the designed FeN3P-SAzyme has a tunable geometry and electronic structure, which is similar to the catalytic kinetics of enzyme. Density functional theory was used to explain the origin of the enzyme activity and substrate specificity. Finally, the authors proved that FeN3P-SAzyme has superior enzyme activity, which can be used as an effective therapeutic strategy to inhibit the growth of tumor cells.


Since the 1950s, the activity of artificial enzyme is far lower than that of natural one, which has been an important scientific problem for a long time. The design and development of artificial enzyme with excellent catalytic performance has always been an important goal of scientific and technological workers. Due to its designable geometric structure and electronic coordination, single-atom nanozyme can effectively simulate the metal active center of natural enzyme at the atomic level. It is one of the most potential candidates to replace natural enzyme, which opens up a new way to develop artificial enzyme with natural enzyme catalytic performance.


The corresponding authors of this article are Prof. LIANG Minmin of Beijing Institute of Technology, Associate Prof. WANG Dingsheng of Tsinghua University, Academician YAN Xiyun of Institute of Biophysics, Chinese Academy of Sciences, and Academician LI Yadong of Tsinghua University.


Rational design of single-atom nanozymes to simulate natural enzymes


Full text link: https://doi.org/10.1038/s41929-021-00609-x


Contact: LIANG Minmin

Institute of Biophysics, Chinese Academy of Sciences

Beijing 100101, China

Email: mmliang@ibp.ac.cn


(Reported by Dr. YAN Xiyun's group)


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