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Deciphering a Nanocarbon‐Based Artificial Peroxidase: Chemical Identification of the Catalytically Active and Substrate‐Binding Sites on Graphene Quantum Dots
Abstract
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.
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Cites
Efficient iterative schemes for ab initio total-energy calculations using a plane-wave basis set
Kresse, G., & Furthmüller, J. (1996) · Physical Review B · doi:10.1103/physrevb.54.11169 · Cited by 123,652
Intrinsic peroxidase-like activity of ferromagnetic nanoparticles
Gao, L., Zhuang, J., Nie, L., Zhang, J., Zhang, Y., Gu, N., Wang, T., Feng, J., Yang, D., Perrett, S., et al. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.260 · Cited by 7,483
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Nanozymes: A clear definition with fuzzy edges
Wei, H., Gao, L., Fan, K., Liu, J., He, J., Qu, X., Dong, S., Wang, E., & Yan, X. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101269 · Cited by 580
Self-citationEnzyme Mimicry for Combating Bacteria and Biofilms
Chen, Z., Wang, Z., Ren, J., & Qu, X. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00011 · Cited by 499
Self-citationUnveiling the active sites of graphene-catalyzed peroxymonosulfate activation
Duan, X., Sun, H., Ao, Z., Zhou, L., Wang, G., & Wang, S. (2016) · Carbon · doi:10.1016/j.carbon.2016.06.016 · Cited by 498
Self-citationNanozymes: Activity origin, catalytic mechanism, and biological application
Yang, W., Yang, X., Zhu, L., Chu, H., Li, X., & Xu, W. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214170 · Cited by 470
Jiang, X.-H., Xing, Q.-J., Luo, X.-B., Li, F., Zou, J.-P., Liu, S.-S., Li, X., & Wang, X.-K. (2018) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2018.01.062 · Cited by 361
Metadata
- Authors
- Sun, H., Zhao, A., Gao, N., Li, K., Ren, J., & Qu, X.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2015-05-04
- Volume
- 54
- Issue
- 24
- Pages
- 7176-7180
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W1905358342
- Cited by
- 529
- References
- 2
- FWCI
- 13.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sun, H., Zhao, A., Gao, N., Li, K., Ren, J., & Qu, X. (2015). Deciphering a Nanocarbon‐Based Artificial Peroxidase: Chemical Identification of the Catalytically Active and Substrate‐Binding Sites on Graphene Quantum Dots. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.201500626
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