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151. A novel catalyst of MIL-101(Fe) doped with Co and Cu as persulfate activator: synthesis, characterization, and catalytic performance.

Author

Duan, Mei-Juan, Guan, Ze-yu, Ma, Yong-Wen, Wan, Jin-Quan, Wang, Yan, and Qu, Yan-Fei

Abstract

In this work, effective and novel heterogeneous catalysts of Metal-organic framework MIL-101(Fe) doped with cobalt (Co) or copper (Cu) have been synthesized by post-synthesis method, namely Co-MIL-101(Fe) and Cu-MIL-101(Fe). The initial and metal-doped samples were tested to activate persulfate (PS) for removal of Acid Orange 7 (AO7) in water. The surface of samples were characterized using X-ray diffraction, Fourier transform infrared spectroscopy, Raman spectroscopy, N adsorption, scanning electron microscopy and transmission electron microscopy. The addition of Cu and Co could alter structure characteristics of MIL-101(Fe) in crystal structure and morphology. The unusual octahedron morphology of MIL-101(Fe) turned to be irregular, disorder and a rod-like morphology was shaped. What is more, Co doping caused greater changes in structure characteristics in comparison with Cu doping. The alteration was reflected in the catalytic capacity of PS activation. An interesting note was that, whether Co or Cu doping, metal-doped MIL-101(Fe) greatly improved the PS activation as compared to unmodified MIL-101(Fe). The removal rate of AO7 was about 66, 92, 98% in MIL-101(Fe)/PS, 6%wtCu-MIL-101(Fe)/PS and 6%wtCo-MIL-101(Fe)/PS system, respectively. Some results also suggested the performance of Co-MIL-101(Fe) was superior to that of Cu-MIL-101(Fe). Additionally, a series of parameters were designed to achieve maximum capacity of PS activation. Such an enhancement in activity may be attributed to the main reasons: the new active sites created by metal additives; an increase in number of active Fe sites produced by Co and Cu doping which results in alteration of morphology and structure of catalysts. [ABSTRACT FROM AUTHOR]

Published
2018
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152. Lipid-Anchored NAC Transcription Factor Is Translocated into the Nucleus and Activates Glyoxalase I Expression during Drought Stress.

Author

Duan, Mei, Zhang, Rongxue, Zhu, Fugui, Zhang, Zhenqian, Gou, Lanming, Wen, Jiangqi, Dong, Jiangli, and Wang, Tao

Subjects
*DROUGHTS, *TRANSCRIPTION factors, *GLYOXALASE, *DROUGHT tolerance, *CELL membranes, *ENDOPLASMIC reticulum
Abstract

The plant-specific NAC (NAM, ATAF1/2, and CUC2) transcription factors (TFs) play a vital role in the response to drought stress. Here, we report a lipid-anchored NACsa TF in Medicago falcata. MfNACsa is an essential regulator of plant tolerance to drought stress, resulting in the differential expression of genes involved in oxidation reduction and lipid transport and localization. MfNACsa is associated with membranes under unstressed conditions and, more specifically, is targeted to the plasma membrane through S -palmitoylation. However, a Cys26-to-Ser mutation or inhibition of S -palmitoylation results in MfNACsa retention in the endoplasmic reticulum/Golgi. Under drought stress, MfNACsa translocates to the nucleus through de- S -palmitoylation mediated by the thioesterase MtAPT1, as coexpression of APT1 results in the nuclear translocation of MfNACsa, whereas mutation of the catalytic site of APT1 results in colocalization with MfNACsa and membrane retention of MfNACsa. Specifically, the nuclear MfNACsa binds the glyoxalase I (MtGlyl) promoter under drought stress, resulting in drought tolerance by maintaining the glutathione pool in a reduced state, and the process is dependent on the APT1-NACsa regulatory module. Our findings reveal a novel mechanism for the nuclear translocation of an S -palmitoylated NAC in response to stress. [ABSTRACT FROM AUTHOR]

Published
2017
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