期刊论文

Yan, Xu(yanx@jlu.edu.cn)

英文

Chemical Engineering Journal

1385-8947

2022

446

136930

10.1016/j.cej.2022.136930

In summary, a new enzyme-mimicking catalyst with densely dispersed accessible atomic copper sites has been designed by simulating the structure of the laccase active center. The coordination microenvironment of the Cu site and electron transfer pathway has been precisely governed by varying the type of peptide, which directly regulated the catalytic activity. In addition, chloride and bromide ion-mediated His-Cys-Cu further produce a high reaction rate and improve adsorption affinity toward the

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Developing enzyme-mimicking catalysts with high catalytic activity and specificity has been a long-standing challenge. Herein we report efficient laccase-mimicking catalysts (His-Cys-Cu) that consist of atomic Cu active centers and dipeptide-organized electron transfer pathway by simulating the catalytic process of natural enzymes, exhibiting high catalytic activity and robust stability. In particular, chloride ion (bromide ions) anchored on the surface of His-Cys-Cu as recognition antenna enhances the catalytic activity and recognition specifi...