A supramolecular metalloenzyme possessing robust oxidase-mimetic catalytic function

Shichao Xu, Haifeng Wu, Siyuan Liu, Peidong Du, Hui Wang (), Haijun Yang, Wenjie Xu, Shuangming Chen, Li Song, Jikun Li, Xinghua Shi and Zhen-Gang Wang ()
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Shichao Xu: Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology
Haifeng Wu: Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology
Siyuan Liu: Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology
Peidong Du: Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology
Hui Wang: National Center for Nanoscience and Technology
Haijun Yang: Tsinghua University
Wenjie Xu: University of Science and Technology of China
Shuangming Chen: University of Science and Technology of China
Li Song: University of Science and Technology of China
Jikun Li: Chinese Academy of Sciences (ICCAS)
Xinghua Shi: National Center for Nanoscience and Technology
Zhen-Gang Wang: Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract Enzymes fold into unique three-dimensional structures to distribute their reactive amino acid residues, but environmental changes can disrupt their essential folding and lead to irreversible activity loss. The de novo synthesis of enzyme-like active sites is challenging due to the difficulty of replicating the spatial arrangement of functional groups. Here, we present a supramolecular mimetic enzyme formed by self-assembling nucleotides with fluorenylmethyloxycarbonyl (Fmoc)-modified amino acids and copper. This catalyst exhibits catalytic functions akin those of copper cluster-dependent oxidases, and catalytic performance surpasses to date-reported artificial complexes. Our experimental and theoretical results reveal the crucial role of periodic arrangement of amino acid components, enabled by fluorenyl stacking, in forming oxidase-mimetic copper clusters. Nucleotides provide coordination atoms that enhance copper activity by facilitating the formation of a copper-peroxide intermediate. The catalyst shows thermophilic behavior, remaining active up to 95 °C in an aqueous environment. These findings may aid the design of advanced biomimetic catalysts and offer insights into primordial redox enzymes.

Date: 2023
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DOI: 10.1038/s41467-023-39779-6

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