Poly(ionic liquid)-derived metal-free heteroatom co-doped porous carbons with peroxidase-like activity

被引:2
作者
Garakani, Sadaf Saeedi [1 ]
Sikdar, Anirban [1 ]
Pang, Kanglei [1 ]
Yuan, Jiayin [1 ]
机构
[1] Stockholm Univ, Dept Mat & Environm Chem, SE-10691 Stockholm, Sweden
基金
瑞典研究理事会;
关键词
Heteroatom co-doped carbon; Metal-free carbonaceous catalyst; Poly(ionic liquid)-derived carbon; Artificial enzyme; Peroxidase-like activity; OXYGEN REDUCTION; GRAPHENE; NANOSHEETS; NANOZYMES; CATALYSTS; NANOPARTICLES; NANOMATERIALS; FACILE; DOTS;
D O I
10.1016/j.apmt.2024.102081
中图分类号
T [工业技术];
学科分类号
08 ;
摘要
Development of affordable, efficient and metal-free heterogeneous catalytic systems has been a persistent challenge in academia and industry. Heteroatom-doped metal-free carbon materials are increasingly recognized as valuable heterogeneous catalysts, and if well-designed, can present comparable performance to, or even surpass transition metal-containing catalysts. Their physicochemical properties and structural characteristics are tunable in a wide range, plus being free of leakage problems of transition metal species into the environment. Herein, three types of hierarchically porous N/X co-doped carbon materials (X denotes B, P or S) were synthesized via using poly(ionic liquid)s (PILs) as carbon precursors and source of heteroatom dopants. The incorporation of sacrificial pore-inducing templating agents which created abundant edge defects, in combination with a heteroatom co-doping strategy, enhanced the number of active sites and their peroxidase-like catalytic activities. Comparison with only nitrogen single-doped porous carbons as reference demonstrated that codoping with nitrogen and another heteroatom exhibits higher peroxidase-like activity and affinity towards substrates. Among the three types of heteroatom co-doped porous carbonaceous artificial enzymes, the N/B codoped carbonaceous catalyst displayed the highest specific activities and Vmax values. These observations suggest a synergistic effect of the co-dopants, here N and B in the enzyme that holds a promising potential to further enhance peroxidase-like activity.
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页数:10
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