Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site. Issue 2 (13th December 2016)

• Record Type: Journal Article
• Authors: Fan, Kelong; Wang, Hui; Xi, Juqun; Liu, Qi; Meng, Xiangqin; Duan, Demin; Gao, Lizeng; Yan, Xiyun
• Is Part Of: Chemical communications. Volume 53:Issue 2(2017)
• Page Start: 424
• Page End: 427
• Publication Date: 2016-12-13
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c6cc08542c
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Histidine modification effectively improved the affinity of Fe3 O4 nanozyme to H2 O2, enhancing its catalytic efficiency by mimicking peroxidase active site. Abstract : The Fe3 O4 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 Fe3 O4 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 Fe3 O4 nanozyme for the substrate H2 O2 and enhanced its catalytic efficiency ( k cat / K M ) up to twenty fold. Thus we not only optimized the activity of the Fe3 O4 nanozyme, but also provide a new rationale for improving the efficiency of nanomaterial-based catalysts by utilizing strategies observed in nature.