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Atom-pair engineering of single-atom nanozyme for boosting peroxidase-like activity.
Wei, Shengjie; Ma, Wenjie; Sun, Minmin; Xiang, Pan; Tian, Ziqi; Mao, Lanqun; Gao, Lizeng; Li, Yadong.
Affiliation
  • Wei S; School of Materials Science and Engineering, Nankai University, Tianjin, 300350, P. R. China.
  • Ma W; Department of Chemistry, Tsinghua University, Beijing, 100084, P. R. China.
  • Sun M; Beijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, The Chinese Academy of Sciences (CAS), Beijing, 100190, P. R. China.
  • Xiang P; College of Animal Science and Technology, Yangzhou University, Yangzhou, 225009, P. R. China.
  • Tian Z; Key Laboratory of Advanced Fuel Cells and Electrolyzers Technology of Zhejiang Province, Ningbo Institute of Materials Technology and Engineering, Chinese Academy of Sciences, Ningbo, 315201, P. R. China.
  • Mao L; Key Laboratory of Advanced Fuel Cells and Electrolyzers Technology of Zhejiang Province, Ningbo Institute of Materials Technology and Engineering, Chinese Academy of Sciences, Ningbo, 315201, P. R. China. tianziqi@nimte.ac.cn.
  • Gao L; College of Chemistry, Beijing Normal University, Beijing, 100875, P. R. China. lqmao@bnu.edu.cn.
  • Li Y; CAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, P. R. China. gaolizeng@ibp.ac.cn.
Nat Commun ; 15(1): 6888, 2024 Aug 12.
Article in En | MEDLINE | ID: mdl-39134525
ABSTRACT
Constructing atom-pair engineering and improving the activity of metal single-atom nanozyme (SAzyme) is significant but challenging. Herein, we design the atom-pair engineering of Zn-SA/CNCl SAzyme by simultaneously constructing Zn-N4 sites as catalytic sites and Zn-N4Cl1 sites as catalytic regulator. The Zn-N4Cl1 catalytic regulators effectively boost the peroxidase-like activities of Zn-N4 catalytic sites, resulting in a 346-fold, 1496-fold, and 133-fold increase in the maximal reaction velocity, the catalytic constant and the catalytic efficiency, compared to Zn-SA/CN SAzyme without the Zn-N4Cl1 catalytic regulator. The Zn-SA/CNCl SAzyme with excellent peroxidase-like activity effectively inhibits tumor cell growth in vitro and in vivo. The density functional theory (DFT) calculations reveal that the Zn-N4Cl1 catalytic regulators facilitate the adsorption of *H2O2 and re-exposure of Zn-N4 catalytic sites, and thus improve the reaction rate. This work provides a rational and effective strategy for improving the peroxidase-like activity of metal SAzyme by atom-pair engineering.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Zinc / Peroxidase Limits: Animals / Humans Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2024 Document type: Article Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Zinc / Peroxidase Limits: Animals / Humans Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2024 Document type: Article Country of publication: