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In this work, quinone-modified metal-organic framework MIL-101(Fe)(Q-MIL-101(Fe)), as a novel heterogeneous Fenton-like catalyst, was synthesized for the activation of persulfate (PS) to remove bisphenol A (BPA). The synthetic Q-MIL-101(Fe) was characterized via X-ray diffraction, scanning electron microscope, Fourier transform infrared, electrochemical impedance spectroscopy, cyclic voltammetry and X-ray photoelectron spectroscopy. As compared to the pure MIL-101(Fe), Q-MIL-101(Fe) displayed better catalytic activity and reusability. The results manifested that the Q-MIL-101(Fe) kept quinone units, which successfully promoted the redox cycling of Fe/Fe and enhanced the removal efficiency. In addition, the reaction factors of Q-MIL-101(Fe) were studied (e.g. pH, catalyst dosage, PS concentration and temperature), showing that the optimum conditions were [catalyst] = 0.2 g/L, [BPA] = 60 mg/L, [PS] = 4 mmol/L, pH = 6.79, temperature = 25 °C. On the basis of these findings, the probable mechanism on the heterogeneous activation of PS by Q-MIL-101(Fe) was proposed.
This article was published in the following journal.
Name: Water science and technology : a journal of the International Association on Water Pollution Research
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In the advanced oxidation system (AOPs) of persulfate (PS) activated by iron-based metal-organic frameworks (MOFs), aim at solving the problem on the treatment difficulty of wastewater with low concen...
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Supramolecular networks that consist of ordered arrangements of organic electron donor linkers (usually ditopic or polytopic organic carboxylates) and metal cations. They can have an extremely high surface area and adjustable pore size that allows for the insertion of other molecules capable of various functions such as catalysis, capture of carbon dioxide, and drug delivery.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 188.8.131.52 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 184.108.40.206 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 220.127.116.11 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
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