4.7 Article

Au nanoparticles on citrate-functionalized graphene nanosheets with a high peroxidase-like performance

Journal

DALTON TRANSACTIONS
Volume 43, Issue 20, Pages 7449-7454

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c3dt53316f

Keywords

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Funding

  1. Japan Society for Promotion of Science (JSPS)
  2. National Natural Science Foundation of China [21305050]
  3. Special Foundation for Young researchers of Health Department of Fujian [2013-2-106]
  4. Scientific Research Foundation of Shangda Li, Jimei University [ZC2013005]
  5. JSPS KAKENHI [2402335, 24550100]
  6. Grants-in-Aid for Scientific Research [12F02335, 24550100] Funding Source: KAKEN

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In this paper, Au nanoparticles (AuNPs) have been homogeneously deposited on citrate-functionalized graphene nanosheets (Cit-GNs) by a simple one-pot reducing method. The morphology and composition of the thus-prepared AuNPs/Cit-GNs were characterized by transmission electron microscopy (TEM), high resolution TEM, energy dispersive X-ray spectroscopy and X-ray photoelectron spectroscopy. The results showed that the AuNPs with a uniform size are well dispersed on the surface of the Cit-GNs. Significantly, the as-prepared AuNPs/Cit-GNs possess intrinsic peroxidase-like activity, which can catalyze the oxidation of the peroxidase substrate 3,3,5,5-tetramethylbenzidine (TMB) by hydrogen peroxide (H2O2) to develop a blue color in aqueous solution. The catalysis was in accordance with Michaelis-Menten kinetics and the AuNPs/Cit-GNs showed a strong affinity for both H2O2 and TMB. Moreover, by comparing with Cit-AuNPs, AuNPs/GNs and AuNPs/PVP-GNs, the AuNPs/Cit-GNs composite exhibits a higher catalytic ability with a lower Michaelis constant (Km) value, suggesting that the GNs with a large surface area and the citrate ions with more carboxyl groups around the AuNPs can greatly enhance the peroxidase-like activity of AuNPs/Cit-GNs. Taking the advantages of the high catalytic activity, the good stability and the low cost, the novel AuNPs/Cit-GNs represent a promising candidate as an enzyme mimic and may find a wide range of new applications in biochemistry and biotechnology.

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