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1D spindle-like iron oxides with controllable phase were synthesized by using MIL-88A-templated pyrolysis under different atmospheres, thermal annealing in N to obtain FeO and in air to obtain α-FeO. Then, 2D/1D core-shell heterostructures (ZnInS@FeO and ZnInS@α-FeO) were constructed by in-situ self-assembly strategy. Characterizations indicated that the 2D ultra-thin ZnInS shell with 0.3 μm was homogeneously coated on the surface of 1D FeO/α-FeO core with 1 μm, and ZnInS@FeO exhibited higher BET surface area (84.5 m g) compared with ZnInS@α-FeO (17.8 m g), providing more exposed active sites and larger contact area. The ZnInS@FeO-5 showed the best photocatalytic activity of RhB degradation as compared to ZnInS, FeO and ZnInS@α-FeO. In addition, the degradation rates of MB, BPA and MO over ZnInS@FeO were much higher than that of ZnInS@α-FeO. The proposed photocatalytic mechanism was also discussed: the FeO as an electron acceptor caused Fe/Fe cycle in ZnInS@FeO and ZnInS@α-FeO followed the Z-scheme mechanism.
This article was published in the following journal.
Name: Journal of hazardous materials
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Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.
Iron or iron compounds used in foods or as food. Dietary iron is important in oxygen transport and the synthesis of the iron-porphyrin proteins hemoglobin, myoglobin, cytochromes, and cytochrome oxidase. Insufficient amounts of dietary iron can lead to iron-deficiency anemia.
Binary compounds of oxygen containing the anion O(2-). The anion combines with metals to form alkaline oxides and non-metals to form acidic oxides.
A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its rate of degradation is increased in the presence of IRON.
A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its RNA binding ability and its aconitate hydrolase activity are dependent upon availability of IRON.