Deciphering a nanocarbon-based artificial peroxidase: chemical identification of the catalytically active and substrate-binding sites on graphene quantum dots.
The design and construction of efficient artificial enzymes is highly desirable. Recent studies have demonstrated that a series of carbon nanomaterials possess intrinsic peroxidase activity. Among them, graphene quantum dots (GQDs) have a high enzymatic activity. However, the catalytic mechanism remains unclear. Therefore, in this report, we chose to decipher their peroxidase activity. By selectively deactivating the ketonic carbonyl, carboxylic, or hydroxy groups and investigating the catalytic activities of these GQD derivatives, we obtained evidence that the -C=O groups were the catalytically active sites, whereas the O=C-O- groups acted as substrate-binding sites, and -C-OH groups can inhibit the activity. These results were corroborated by theoretical studies. This work should not only enhance our understanding of nanocarbon-based artificial enzymes, but also facilitate the design and construction of other types of target-specific artificial enzymes.
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022 (China).|University of Chinese Academy of Science, Beijing, 100039 (China).
Hanjun
H
Sun
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022 (China).|University of Chinese Academy of Science, Beijing, 100039 (China).
Andong
A
Zhao
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022 (China).
Nan
N
Gao
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022 (China).
Kai
K
Li
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022 (China).
Jinsong
J
Ren
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022 (China). xqu@ciac.ac.cn.
Xiaogang
X
Qu
D001565:Benzoates / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D020134:Catalytic Domain; D006108:Graphite / Q000737:chemistry*; D063086:Organothiophosphates / Q000737:chemistry; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism; D010659:Phenylhydrazines / Q000737:chemistry / Q000378:metabolism; D045663:Quantum Dots / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
D001565:Benzoates; D063086:Organothiophosphates; D010659:Phenylhydrazines; C030299:phenylhydrazine; C100092:bromophos; D006108:Graphite; C102988:benzoic anhydride; D009195:Peroxidase
catalysis; graphene quantum dots; nanoparticles; peroxidase activity; reaction mechanisms