Issue 82, 2017

Mimicking horseradish peroxidase and oxidase using ruthenium nanomaterials

Abstract

Although important progress has been achieved for the study of noble metal-based enzyme-like catalysts, there are rare reports on the enzyme mimicking applications of ruthenium nanoparticles (Ru NPs). In this work, we investigated the horseradish peroxidase (HRP) and oxidase mimetic activity of Ru NPs. Mimicking HRP, Ru NPs could catalyze the oxidation of substrates 3,3,5,5-tetramethylbenzidine (TMB), o-phenylenediamine (OPD) and dopamine hydrochloride (DA) in the presence of exogenously added H2O2 to generate the products with blue, yellow and orange colors, respectively. We also report the first evidence that Ru NPs possess intrinsic oxidase-like activity, which could catalyze the oxidization of TMB and sodium L-ascorbate (NaA) by dissolved oxygen. The HRP-like and oxidase-like activities of Ru NPs were found to be related to the concentrations of Ru NPs. The catalytic mechanism was analyzed by electron spin resonance spectroscopy (ESR), which suggested that the enzyme mimicking activities of the Ru NPs might originate from their characteristic of accelerating electron transfer between substrates and H2O2 or O2. Our findings offer a better understanding of enzyme-mimicking Ru NPs and should provide important insights for future applications.

Graphical abstract: Mimicking horseradish peroxidase and oxidase using ruthenium nanomaterials

Supplementary files

Article information

Article type
Paper
Submitted
18 Sep 2017
Accepted
06 Nov 2017
First published
10 Nov 2017
This article is Open Access
Creative Commons BY license

RSC Adv., 2017,7, 52210-52217

Mimicking horseradish peroxidase and oxidase using ruthenium nanomaterials

G. Cao, X. Jiang, H. Zhang, T. R. Croley and J. Yin, RSC Adv., 2017, 7, 52210 DOI: 10.1039/C7RA10370K

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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