title: Optimization of Fe3O4nanozyme activity via single amino acid modification mimicking an enzyme active site.
abstract: The Fe3O4nanozyme 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 Fe3O4nanoparticle 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 (KM) of the Fe3O4nanozyme for the substrate H2O2and enhanced its catalytic efficiency (kcat/KM) up to twenty fold. Thus we not only optimized the activity of the Fe3O4nanozyme, but also provide a new rationale for improving the efficiency of nanomaterial-based catalysts by utilizing strategies observed in nature.
authors.affiliation: 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.
authors.forename: Kelong
authors.initials: K
authors.lastname: Fan
authors.affiliation: CAS Key Laboratory of Nanosystem and Hierarchical Fabrication, National Centre for Nanoscience and Technology, Beijing 100190, China.
authors.forename: Hui
authors.initials: H
authors.lastname: Wang
authors.affiliation: School of Medicine, Yangzhou University, Yangzhou, Jiangsu 225001, China.
authors.forename: Juqun
authors.initials: J
authors.lastname: Xi
authors.affiliation: School of Medicine, Yangzhou University, Yangzhou, Jiangsu 225001, China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Liu
authors.affiliation: 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.
authors.forename: Xiangqin
authors.initials: X
authors.lastname: Meng
authors.affiliation: 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.
authors.forename: Demin
authors.initials: D
authors.lastname: Duan
authors.affiliation: 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.
authors.forename: Lizeng
authors.initials: L
authors.lastname: Gao
authors.affiliation: 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.
authors.forename: Xiyun
authors.initials: X
authors.lastname: Yan
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D020134:Catalytic Domain; D005290:Ferric Compounds / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000737:chemistry; D008958:Models, Molecular; D053758:Nanoparticles / Q000737:chemistry*
chemical_list: D005290:Ferric Compounds; C000499:ferric oxide; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase