Publication | Closed Access
Mimicking Peroxidase Activities with Prussian Blue Nanoparticles and Their Cyanometalate Structural Analogues
129
Citations
22
References
2017
Year
Nanoparticles composed of Prussian Blue, PB, and the cyanometalate structural analogues, CuFe, FeCoFe, and FeCo, are examined as inorganic clusters that mimic the functions of peroxidases. PB acts as a superior catalyst for the oxidation of dopamine to aminochrome by H<sub>2</sub>O<sub>2</sub>. The oxidation of dopamine by H<sub>2</sub>O<sub>2</sub> in the presence of PB is 6-fold faster than in the presence of CuFe. The cluster FeCo does not catalyze the oxidation of dopamine to aminochrome. The most efficient catalyst for the generation of chemiluminescence by the oxidation of luminol by H<sub>2</sub>O<sub>2</sub> is, however, FeCo, and PB lacks any catalytic activity toward the generation of chemiluminescence. The order of catalyzed chemiluminescence generation is FeCo ≫ CuFe > FeCoFe. The clusters PB, CuFe, FeCoFe, and FeCo mimic the functions of NADH peroxidase. The catalyzed oxidation of NADH by H<sub>2</sub>O<sub>2</sub> to form NAD<sup>+</sup> follows the order PB ≫ CuFe ∼ FeCoFe, FeCo. The efficient generation of chemiluminescence by the FeCo-catalyzed oxidation of luminol by H<sub>2</sub>O<sub>2</sub> is used to develop a glucose sensor. The aerobic oxidation of glucose in the presence of glucose oxidase, GOx, yields gluconic acid and H<sub>2</sub>O<sub>2</sub>. The chemiluminescence intensities formed by the GOx-generated H<sub>2</sub>O<sub>2</sub> relate to the concentration of glucose, thus providing a quantitative readout signal for the concentrations of glucose.
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