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

Kelong Fan; Hui Wang; Juqun Xi; Qi Liu; Xiangqin Meng; Demin Duan; Lizeng Gao; Xiyun Yan

doi:10.1039/c6cc08542c

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

Chem Commun (Camb). 2016 Dec 22;53(2):424-427. doi: 10.1039/c6cc08542c.

Authors

Kelong Fan¹, Hui Wang², Juqun Xi³, Qi Liu³, Xiangqin Meng⁴, Demin Duan¹, Lizeng Gao⁵, Xiyun Yan⁴

Affiliations

¹ 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. lzgao@yzu.edu.cn yanxy@ibp.ac.cn.
² CAS Key Laboratory of Nanosystem and Hierarchical Fabrication, National Centre for Nanoscience and Technology, Beijing 100190, China.
³ School of Medicine, Yangzhou University, Yangzhou, Jiangsu 225001, China.
⁴ 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. lzgao@yzu.edu.cn yanxy@ibp.ac.cn and University of Chinese Academy of Sciences, Beijing 100049, China.
⁵ 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. lzgao@yzu.edu.cn yanxy@ibp.ac.cn and School of Medicine, Yangzhou University, Yangzhou, Jiangsu 225001, China.

PMID: 27959363
DOI: 10.1039/c6cc08542c

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Biomimetic Materials / chemistry*
Catalytic Domain*
Ferric Compounds / chemistry*
Horseradish Peroxidase / chemistry*
Horseradish Peroxidase / metabolism*
Hydrogen Peroxide / chemistry
Models, Molecular
Nanoparticles / chemistry*

Substances

Ferric Compounds
ferric oxide
Hydrogen Peroxide
Horseradish Peroxidase