Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site (original) (raw)
* Corresponding authors
a Key Laboratory of Protein and Peptide Pharmaceuticals, CAS-University of Tokyo Joint Laboratory of Structural Virology and Immunology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
E-mail: lzgao@yzu.edu.cn, yanxy@ibp.ac.cn
Tel: +86-514-87797090
b CAS Key Laboratory of Nanosystem and Hierarchical Fabrication, National Centre for Nanoscience and Technology, Beijing 100190, China
c School of Medicine, Yangzhou University, Yangzhou, Jiangsu 225001, China
d University of Chinese Academy of Sciences, Beijing 100049, China
Abstract
The Fe3O4 nanozyme was the first reported nanoparticle with intrinsic peroxidase-like activity and has been widely used in biomedicine. To optimize its catalytic activity, we introduced histidine residues onto the Fe3O4 nanoparticle surface in order to mimic the enzymatic microenvironment of natural peroxidase enzymes. Our results show that modification with a single amino acid could more than ten-fold improve the apparent affinity (_K_M) of the Fe3O4 nanozyme for the substrate H2O2 and enhanced its catalytic efficiency (_k_cat/_K_M) up to twenty fold. Thus we not only optimized the activity of the Fe3O4 nanozyme, but also provide a new rationale for improving the efficiency of nanomaterial-based catalysts by utilizing strategies observed in nature.
You have access to this article
Please wait while we load your content... Something went wrong. Try again?
Supplementary files
Article information
DOI
https://doi.org/10.1039/C6CC08542C
Article type
Communication
Submitted
24 Oct 2016
Accepted
02 Dec 2016
First published
02 Dec 2016
Download Citation
Chem. Commun., 2017,53, 424-427
Permissions
Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site
K. Fan, H. Wang, J. Xi, Q. Liu, X. Meng, D. Duan, L. Gao and X. Yan,Chem. Commun., 2017, 53, 424DOI: 10.1039/C6CC08542C
To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.
If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.
If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.
Read more about how to correctly acknowledge RSC content.