Aggregation-induced accelerating peroxidase-like activity of gold nanoclusters and their applications for colorimetric Pb<sup>2+</sup> detection

Liao, Hong; Liu, Guangjuan; Liu, Yun; Rong, Li; Fu, Wensheng; Hu, Lianzhe

doi:10.1039/c7cc05409b

Cited by 109 publications

(46 citation statements)

References 26 publications

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“…AuNPs, one of the most widely studied NPs, have been regarded as a highly inert nanomaterial . Recently, they have been found to exhibit surprising enzyme‐mimicking activities when decorated with different surface modifications . For instance, citrate‐coated AuNPs mimic glucose oxidase (GOx) .…”

Section: Figurementioning

confidence: 99%

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Hafez

2019

Angew Chem Int Ed

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Gold nanoparticles (AuNPs) have been demonstrated to serve as effective nanomaterial‐based enzyme mimetics (nanozymes) for a number of enzymatic reactions under mild conditions. The intrinsic glucose oxidase and peroxidase activities of single AuNPs and Ag–Au nanohybrids, respectively, were investigated by single NP collision electrochemical measurements. A significantly high turnover number of nanozymes was obtained from individual catalytic events compared with the results from the classical, ensemble‐averaged measurements. The unusual enhancement of catalytic activity of single nanozymes is believed to originate from the high accessible surface area of monodispersed NPs and the high activities of carbon‐supported NPs during single‐particle collision at a carbon ultramicroelectrode. This work introduces a new method for the precise characterization of the intrinsic catalytic activities of nanozymes, giving further insights to the design of high‐efficiency nanomaterial catalysts.

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Section: Figurementioning

confidence: 99%

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Hafez

2019

Angew Chem Int Ed

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“…[10][11][12][13] AuNPs,o ne of the most widely studied NPs,h ave been regarded as ah ighly inert nanomaterial. [5,8,[15][16][17][18][19][20][21][22] Fori nstance,c itrate-coated AuNPs mimic glucose oxidase (GOx). [5,8,[15][16][17][18][19][20][21][22] Fori nstance,c itrate-coated AuNPs mimic glucose oxidase (GOx).…”

mentioning

confidence: 99%

“…[14] Recently,t hey have been found to exhibit surprising enzyme-mimicking activities when decorated with different surface modifications. [5,8,[15][16][17][18][19][20][21][22] Fori nstance,c itrate-coated AuNPs mimic glucose oxidase (GOx). [18][19][20] Furthermore,changing the capping molecule or the adsorption of metal ions (for example,Hg 2+ , Bi 3+ ,Ag + ,Pb 2+ )onthe surface of the AuNPs could alter their enzyme-like activities,t hat is,s witch their activity to perox-idase nanomimetics.…”

mentioning

confidence: 99%

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Hafez

et al. 2019

Angewandte Chemie

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Gold nanoparticles (AuNPs) have been demonstrated to serve as effective nanomaterial-based enzyme mimetics (nanozymes) for an umber of enzymatic reactions under mild conditions.T he intrinsic glucose oxidase and peroxidase activities of single AuNPs and Ag-Au nanohybrids, respectively,w ere investigated by single NP collision electrochemical measurements.Asignificantly high turnover number of nanozymes was obtained from individual catalytic events compared with the results from the classical, ensembleaveraged measurements.The unusual enhancement of catalytic activity of single nanozymes is believed to originate from the high accessible surface area of monodispersed NPs and the high activities of carbon-supported NPs during single-particle collision at acarbon ultramicroelectrode.This work introduces an ew method for the precise characterization of the intrinsic catalytic activities of nanozymes,g iving further insights to the design of high-efficiency nanomaterial catalysts.

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“…In the literature, thiols are well known to poison the surface of AuNPs (i.e., catalytic deactivation) due to the formation of strong Au-S bonds [29,30]. Cysteamine with the -SH group could oxidize superficial gold atoms (i.e., Au(0)) after binding to AuNP surface, resulting in a significant contribution to inaccessible Au(I) because such Au(I)-thiolate complexes are inactive catalytically [31]. Accordingly, the Au(0) and Au(I) on the surface are both indispensable for the peroxidase-like activity of AuNPs.…”

Section: Discussionmentioning

confidence: 99%

Revealing the Active Site of Gold Nanoparticles for the Peroxidase-Like Activity: The Determination of Surface Accessibility

Liu

Chen

et al. 2019

Catalysts

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Despite the fact that the enzyme-like activities of nanozymes (i.e., nanomaterial-based artificial enzymes) are highly associated with their surface properties, little is known about the catalytic active sites. Here, we used the sulfide ion (S2−)-induced inhibition of peroxidase-like activity to explore active sites of gold nanoparticles (AuNPs). The inhibition mechanism was based on the interaction with Au(I) to form Au2S, implying that the Au(I) might be the active site of AuNPs for the peroxidase-like activity. X-ray photoelectron spectroscopy (XPS) analysis showed that the content of Au(I) on the surface of AuNPs significantly decreased after the addition of S2−, which might be contributed to the more covalent Au–S bond in the formation of Au2S. Importantly, the variations of Au(I) with and without the addition of S2− for different surface-capped AuNPs were in good accordance with their corresponding peroxidase-like activities. These results confirmed that the accessible Au(I) on the surface was the main requisite for the peroxidase-like activity of AuNPs for the first time. In addition, the use of S2− could assist to determine available active sites for different surface modified AuNPs. This work not only provides a new method to evaluate the surface accessibility of colloidal AuNPs but also gains insight on the design of efficient AuNP-based peroxidase mimics.

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Aggregation-induced accelerating peroxidase-like activity of gold nanoclusters and their applications for colorimetric Pb²⁺ detection

Cited by 109 publications

References 26 publications

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Revealing the Active Site of Gold Nanoparticles for the Peroxidase-Like Activity: The Determination of Surface Accessibility

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Aggregation-induced accelerating peroxidase-like activity of gold nanoclusters and their applications for colorimetric Pb2+ detection

Cited by 109 publications

References 26 publications

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Unveiling the Intrinsic Catalytic Activities of Single‐Gold‐Nanoparticle‐Based Enzyme Mimetics

Revealing the Active Site of Gold Nanoparticles for the Peroxidase-Like Activity: The Determination of Surface Accessibility

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Aggregation-induced accelerating peroxidase-like activity of gold nanoclusters and their applications for colorimetric Pb²⁺ detection