Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site-Reference-Cited by-同舟云学术

Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site

Published:2017 Issue:2 Volume:53 Page:424-427
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Fan Kelong¹²³⁴⁵,Wang Hui⁶⁷⁸⁹,Xi Juqun¹⁰¹¹¹²⁹,Liu Qi¹⁰¹¹¹²⁹,Meng Xiangqin¹²³⁴⁵,Duan Demin¹²³⁴⁵,Gao Lizeng¹²³⁴⁵,Yan Xiyun¹²³⁴⁵

Affiliation:

1. Key Laboratory of Protein and Peptide Pharmaceuticals

2. CAS-University of Tokyo Joint Laboratory of Structural Virology and Immunology

3. Institute of Biophysics

4. Chinese Academy of Sciences

5. Beijing 100101

6. CAS Key Laboratory of Nanosystem and Hierarchical Fabrication

7. National Centre for Nanoscience and Technology

8. Beijing 100190

9. China

10. School of Medicine

11. Yangzhou University

12. Yangzhou

Abstract

Histidine modification effectively improved the affinity of Fe₃O₄ nanozyme to H₂O₂, enhancing its catalytic efficiency by mimicking peroxidase active site.

Funder

Natural Science Foundation of Beijing Municipality

China Postdoctoral Science Foundation

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CC/C6CC08542C

Reference25 articles.

1. Nanozymes: an emerging field bridging nanotechnology and biology

2. Nanomaterials with enzyme-like characteristics (nanozymes): next-generation artificial enzymes

3. Catalytically Active Nanomaterials: A Promising Candidate for Artificial Enzymes

4. Nanozymes in bionanotechnology: from sensing to therapeutics and beyond

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