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Issue 2, 2017
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Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site

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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 (KM) of the Fe3O4 nanozyme for the substrate H2O2 and enhanced its catalytic efficiency (kcat/KM) 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.

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

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Publication details

The article was received on 24 Oct 2016, accepted on 02 Dec 2016 and first published on 02 Dec 2016


Article type: Communication
DOI: 10.1039/C6CC08542C
Citation: Chem. Commun., 2017,53, 424-427
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    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, 424
    DOI: 10.1039/C6CC08542C

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