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Control of Stepwise Hg 2+ Reduction on Gold to Selectively Tune its Peroxidase and Catalase‐Like Activities and the Mechanism
Author(s) -
Chen Yao,
Shen Xiaomei,
Carmona Unai,
Yang Fan,
Gao Xingfa,
Knez Mato,
Zhang Lianbing,
Qin Yong
Publication year - 2021
Publication title -
advanced materials interfaces
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.671
H-Index - 65
ISSN - 2196-7350
DOI - 10.1002/admi.202100086
Subject(s) - catalase , peroxidase , enzyme , passivity , chemistry , amalgam (chemistry) , materials science , combinatorial chemistry , biochemistry , electrode , electrical engineering , engineering
The flexible regulation of enzyme‐like activities of nanozyme is of great importance in biomedical applications. However, the current modulation strategies usually lack activity specificity to reveal precise tuning of the desired activity. In this work, it is demonstrated for the first time that the Hg 2+ on surfaces of Au film can be reduced in a chemical path of Hg(II) → Hg(I) → Hg(0) via anti‐Galvanic reaction. Furthermore, it is amazing that the generated Hg 0 via Hg(NO 3 ) 2 treatment contributes to greatly boosted peroxidase and catalase activities of Au films due to the formation of Au@Hg amalgam, while the main Hg + species on Au formed by HgCl 2 modification results in only catalase‐like activity acceleration. Based on this, the peroxidase‐ and catalase‐like activities of gold can be selectively modulated by controlling the stepwise reduction of Hg 2+ . Further density functionality theory (DFT) calculations reveal that it is the significantly lowered activation energy by Au@Hg amalgam that accounts for the acceleration of both peroxidase and catalase reaction. These results demonstrate a novel avenue to specifically modulate the enzyme‐mimicking activities of Au, which not only facilitates the design of nanozymes with specific activity, but also broadens their biological usage.