Atomic-scale strain engineering of atomically resolved Pt clusters transcending natural enzymes
Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt 1 ), several Pt atoms (Pt n...
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| Published in | Nature communications Vol. 15; no. 1; pp. 8346 - 18 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
27.09.2024
Nature Publishing Group Nature Portfolio |
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| Abstract | Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt
1
), several Pt atoms (Pt
n
) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the
d
-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (
K
cat
/
K
m
) of 1.50 × 10
9
mM
−1
min
−1
, about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder.
Strain engineering is promising for improving catalytic capability of biocatalysts, but it is challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, the authors report the biocatalysts with atomically-resolved Pt clusters laminated on PdAu nanocrystals and show that the tensile strains contribute to the enzyme-like activities greater than that of natural enzymes. |
|---|---|
| AbstractList | Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt1), several Pt atoms (Ptn) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (Kcat/Km) of 1.50 × 109 mM−1 min−1, about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder.Strain engineering is promising for improving catalytic capability of biocatalysts, but it is challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, the authors report the biocatalysts with atomically-resolved Pt clusters laminated on PdAu nanocrystals and show that the tensile strains contribute to the enzyme-like activities greater than that of natural enzymes. Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt1), several Pt atoms (Ptn) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (Kcat/Km) of 1.50 × 109 mM-1 min-1, about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder.Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt1), several Pt atoms (Ptn) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (Kcat/Km) of 1.50 × 109 mM-1 min-1, about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder. Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt 1 ), several Pt atoms (Pt n ) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d -band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency ( K cat / K m ) of 1.50 × 10 9 mM −1 min −1 , about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder. Strain engineering is promising for improving catalytic capability of biocatalysts, but it is challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, the authors report the biocatalysts with atomically-resolved Pt clusters laminated on PdAu nanocrystals and show that the tensile strains contribute to the enzyme-like activities greater than that of natural enzymes. Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt ), several Pt atoms (Pt ) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (K /K ) of 1.50 × 10 mM min , about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder. Abstract Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt1), several Pt atoms (Ptn) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (K cat/K m) of 1.50 × 109 mM−1 min−1, about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder. |
| ArticleNumber | 8346 |
| Author | Zhao, Shuang Ren, Qinjuan Fu, Yikai Yang, Jingkai Zhao, Ruoli Cao, Yang Zhang, Bo Dai, Haitao Xin, Qi Li, Yonghui Luo, Ran Yan, Yuxing Chang, Jin Liu, Ling Gong, Xiaoqun Qin, Qiong Liu, Qingshan Ren, Yaoyao Zhang, Xiao-Dong Yao, Peiyu Chen, Ke Mu, Xiaoyu Li, Yuan Li, Guo Liu, Changlong Long, Wei Zhang, Jianning Zhang, Shu Wang, Junying Liu, Shu-Lin |
| Author_xml | – sequence: 1 givenname: Ke surname: Chen fullname: Chen, Ke organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University – sequence: 2 givenname: Guo surname: Li fullname: Li, Guo organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 3 givenname: Xiaoqun surname: Gong fullname: Gong, Xiaoqun organization: School of Life Sciences, Tianjin Engineering Center of Micro-Nano Biomaterials and Detection-Treatment Technology, Tianjin University – sequence: 4 givenname: Qinjuan surname: Ren fullname: Ren, Qinjuan organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 5 givenname: Junying surname: Wang fullname: Wang, Junying organization: Lineberger Comprehensive Cancer Center, School of Medicine, University of North Carolina at Chapel Hill – sequence: 6 givenname: Shuang surname: Zhao fullname: Zhao, Shuang organization: School of Life Sciences, Tianjin Engineering Center of Micro-Nano Biomaterials and Detection-Treatment Technology, Tianjin University – sequence: 7 givenname: Ling surname: Liu fullname: Liu, Ling organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University – sequence: 8 givenname: Yuxing surname: Yan fullname: Yan, Yuxing organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University – sequence: 9 givenname: Qingshan surname: Liu fullname: Liu, Qingshan organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University – sequence: 10 givenname: Yang surname: Cao fullname: Cao, Yang organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University – sequence: 11 givenname: Yaoyao surname: Ren fullname: Ren, Yaoyao organization: Tianjin Neurological Institute, Department of Neurosurgery, Tianjin Medical University General Hospital – sequence: 12 givenname: Qiong surname: Qin fullname: Qin, Qiong organization: Tianjin Neurological Institute, Department of Neurosurgery, Tianjin Medical University General Hospital – sequence: 13 givenname: Qi surname: Xin fullname: Xin, Qi organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University – sequence: 14 givenname: Shu-Lin orcidid: 0000-0002-1043-4238 surname: Liu fullname: Liu, Shu-Lin organization: State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Centre for New Organic Matter, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Centre for Analytical Sciences, College of Chemistry, School of Medicine and Frontiers Science Center for Cell Responses, Nankai University – sequence: 15 givenname: Peiyu surname: Yao fullname: Yao, Peiyu organization: State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Centre for New Organic Matter, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Centre for Analytical Sciences, College of Chemistry, School of Medicine and Frontiers Science Center for Cell Responses, Nankai University – sequence: 16 givenname: Bo orcidid: 0000-0001-8745-2752 surname: Zhang fullname: Zhang, Bo organization: Department of Biomedical Engineering, Southern University of Science and Technology – sequence: 17 givenname: Jingkai surname: Yang fullname: Yang, Jingkai organization: Department of Biomedical Engineering, Southern University of Science and Technology – sequence: 18 givenname: Ruoli surname: Zhao fullname: Zhao, Ruoli organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 19 givenname: Yuan surname: Li fullname: Li, Yuan organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 20 givenname: Ran surname: Luo fullname: Luo, Ran organization: School of Life Sciences, Tianjin Engineering Center of Micro-Nano Biomaterials and Detection-Treatment Technology, Tianjin University – sequence: 21 givenname: Yikai surname: Fu fullname: Fu, Yikai organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 22 givenname: Yonghui orcidid: 0000-0002-6105-6484 surname: Li fullname: Li, Yonghui organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 23 givenname: Wei surname: Long fullname: Long, Wei organization: Tianjin Key Laboratory of Molecular Nuclear Medicine, Institute of Radiation Medicine Chinese Academy of Medical, Sciences and Peking Union Medical College – sequence: 24 givenname: Shu surname: Zhang fullname: Zhang, Shu organization: Tianjin Neurological Institute, Department of Neurosurgery, Tianjin Medical University General Hospital – sequence: 25 givenname: Haitao surname: Dai fullname: Dai, Haitao organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 26 givenname: Changlong surname: Liu fullname: Liu, Changlong organization: Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 27 givenname: Jianning orcidid: 0000-0003-3627-863X surname: Zhang fullname: Zhang, Jianning organization: Tianjin Neurological Institute, Department of Neurosurgery, Tianjin Medical University General Hospital – sequence: 28 givenname: Jin surname: Chang fullname: Chang, Jin organization: School of Life Sciences, Tianjin Engineering Center of Micro-Nano Biomaterials and Detection-Treatment Technology, Tianjin University – sequence: 29 givenname: Xiaoyu orcidid: 0000-0002-6053-9775 surname: Mu fullname: Mu, Xiaoyu email: muxiaoyu@tju.edu.cn organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University, Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University – sequence: 30 givenname: Xiao-Dong orcidid: 0000-0002-7212-0138 surname: Zhang fullname: Zhang, Xiao-Dong email: xiaodongzhang@tju.edu.cn organization: Tianjin Key Laboratory of Brain Science and Neural Engineering, Academy of Medical Engineering and Translational Medicine, Tianjin University, Department of Physics and Tianjin Key Laboratory of Low Dimensional Materials Physics and Preparing Technology, School of Sciences, Tianjin University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39333142$$D View this record in MEDLINE/PubMed |
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| Title | Atomic-scale strain engineering of atomically resolved Pt clusters transcending natural enzymes |
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