Deciphering the catalytic mechanism of superoxide dismutase activity of carbon dot nanozyme
Xi'an Jiaotong University · Chinese Academy of Sciences · +7 more institutions
Abstract
Nanozymes with superoxide dismutase (SOD)-like activity have attracted increasing interest due to their ability to scavenge superoxide anion, the origin of most reactive oxygen species in vivo. However, SOD nanozymes reported thus far have yet to approach the activity of natural enzymes. Here, we report a carbon dot (C-dot) SOD nanozyme with a catalytic activity of over 10,000 U/mg, comparable to that of natural enzymes. Through selected chemical modifications and theoretical calculations, we show that the SOD-like activity of C-dots relies on the hydroxyl and carboxyl groups for binding superoxide anions and the carbonyl groups conjugated with the π-system for electron transfer. Moreover, C-dot SOD nanozymes…
Citation impact
- FWCI
- 50.37
- Percentile
- 100%
- References
- 66
Authors
13Topics & keywords
- Superoxide dismutase
- Mechanism (biology)
- Catalysis
- Chemistry
- Superoxide
- Biochemistry
- Enzyme
- Physics
Funding
- NNNational Natural Science Foundation of ChinaAwards: 81930050, 21805021, 82101411, 82000523, 82122037, 32171392
- CAChinese Academy of SciencesAwards: JCTD-2020-08, 2019093
- CPChina Postdoctoral Science FoundationAward: 2020M683449
- YIYouth Innovation Promotion Association of the Chinese Academy of SciencesAwards: 2019093, JCTD-2020-08
- NSNatural Science Foundation of Shaanxi ProvinceAward: 2021JQ-009
- NKNational Key Research and Development Program of ChinaAward: 2021YFC2102900
- YIYouth Innovation Promotion AssociationAward: 2019093
- IOInstitute of Biophysics, Chinese Academy of Sciences