期刊
JACS AU
卷 2, 期 11, 页码 2453-2459出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacsau.2c00495
关键词
defect; amorphous; noble metal; peroxidase nanozyme; specificity
资金
- National Science Fund for Distinguished Young Scholars [52025133]
- National Key R&D Program of China [2019YFA0709202]
- Tencent Foundation through the XPLORER PRIZE
- Beijing Natural Science Foundation [JQ18005]
- Fund of the State Key Laboratory of Solidification Processing in NWPU [SKLSP202004]
- Youth Innovation Promotion Association [202055]
- National Natural Science Foundation of China [22105007]
- China Postdoctoral Science Foundation [2020M670018]
This study reports the synthesis of amorphous/crystalline PtRuTe nanozymes with selectively enhanced peroxidase-like activity and suppressed oxidase-like activity. The amorphous domains play a critical role in tuning and optimizing the catalytic properties, and the high-percentage defects of the PtRuTe nanozyme exhibit superior catalytic activities and kinetics.
Noble metal based nanozymes show great potential in replacing natural enzymes; however, their development is greatly restricted by their relatively low specificity and activity. Herein, we report the synthesis of a class of amorphous/crystalline PtRuTe nanomaterials with a Pt/Te-enriched core and a Ru-enriched shell as efficient peroxidase mimics with selectively enhanced perox-idase-like activity and suppressed oxidase-like activity. We demonstrate that amorphous domains play a critical role in tuning and optimizing the catalytic properties. The PtRuTe nanozyme with high-percentage defects exhibits superior catalytic activities and kinetics, and the suppressed oxidase-like activity could diminish the interference of O2 in the glucose colorimetric assay. The high catalytic performance can be caused by amorphous phase induced electron redistribution and electronic interactions between different elements and the synergistic effect of multimetallic nanocrystals. The concurrent extraordinary peroxidase-like activity and suppressed oxidase-like activity guarantee the amorphous/crystalline PtRuTe nanozymes as promising alternatives of natural enzymes for biosensing and beyond.
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