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Deciphering a Nanocarbon‐Based Artificial Peroxidase: Chemical Identification of the Catalytically Active and Substrate‐Binding Sites on Graphene Quantum Dots
Author(s) -
Sun Hanjun,
Zhao Andong,
Gao Nan,
Li Kai,
Ren Jinsong,
Qu Xiaogang
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201500626
Subject(s) - graphene , artificial enzyme , peroxidase , substrate (aquarium) , chemistry , catalysis , nanomaterials , enzyme , active site , combinatorial chemistry , nanotechnology , stereochemistry , organic chemistry , materials science , biology , ecology
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 CO groups were the catalytically active sites, whereas the OCO groups acted as substrate‐binding sites, and COH 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.