Metal-ligand dual-site single-atom nanozyme mimicking urate oxidase with high substrates specificity

Kaiyuan Wang, Qing Hong, Caixia Zhu, Yuan Xu, Wang Li, Ying Wang, Wenhao Chen, Xiang Gu, Xinghua Chen, Yanfeng Fang, Yanfei Shen (), Songqin Liu and Yuanjian Zhang ()
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Kaiyuan Wang: School of Chemistry and Chemical Engineering
Qing Hong: School of Chemistry and Chemical Engineering
Caixia Zhu: School of Chemistry and Chemical Engineering
Yuan Xu: School of Chemistry and Chemical Engineering
Wang Li: School of Chemistry and Chemical Engineering
Ying Wang: School of Chemistry and Chemical Engineering
Wenhao Chen: School of Chemistry and Chemical Engineering
Xiang Gu: School of Chemistry and Chemical Engineering
Xinghua Chen: School of Chemistry and Chemical Engineering
Yanfeng Fang: School of Chemistry and Chemical Engineering
Yanfei Shen: Southeast University
Songqin Liu: School of Chemistry and Chemical Engineering
Yuanjian Zhang: School of Chemistry and Chemical Engineering

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract In nature, coenzyme-independent oxidases have evolved in selective catalysis using isolated substrate-binding pockets. Single-atom nanozymes (SAzymes), an emerging type of non-protein artificial enzymes, are promising to simulate enzyme active centers, but owing to the lack of recognition sites, realizing substrate specificity is a formidable task. Here we report a metal-ligand dual-site SAzyme (Ni-DAB) that exhibited selectivity in uric acid (UA) oxidation. Ni-DAB mimics the dual-site catalytic mechanism of urate oxidase, in which the Ni metal center and the C atom in the ligand serve as the specific UA and O2 binding sites, respectively, characterized by synchrotron soft X-ray absorption spectroscopy, in situ near ambient pressure X-ray photoelectron spectroscopy, and isotope labeling. The theoretical calculations reveal the high catalytic specificity is derived from not only the delicate interaction between UA and the Ni center but also the complementary oxygen reduction at the beta C site in the ligand. As a potential application, a Ni-DAB-based biofuel cell using human urine is constructed. This work unlocks an approach of enzyme-like isolated dual sites in boosting the selectivity of non-protein artificial enzymes.

Date: 2024
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DOI: 10.1038/s41467-024-50123-4

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