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        Graphitic carbon nitride embedded Ni3(VO4)2/ZnCr2O4 Z-scheme photocatalyst for efficient degradation of p-chlorophenol and 5-fluorouracil, and genotoxic evaluation in Allium cepa

        M. Swedha,Abdulrahman A. Alatar,Mohammad K. Okla,Ibrahim A. Alaraidh,Asmaa Mohebaldin,Mohammed Aufy,Lija L. Raju,Ajith M. Thomas,Mostafa A. Abdel-Maksoud,S. Sudheer Khan 한국공업화학회 2022 Journal of Industrial and Engineering Chemistry Vol.112 No.-

        Visible light photocatalysis using nano heterostructures offers an eco-friendly alternative for the removalof organic molecules. Here, we reported an enhanced photocatalytic activity of g-C3N4/Ni3(VO4)2/ZnCr2O4, a dual Z-scheme nano-heterojunction for the photocatalytic removal of p-chlorophenol (p-CP)and 5-fluorouracil (5-FU). The nano heterojunction was fabricated by a facile co-precipitation method. Initially, the fabricated nanocomposites (NCs) were characterized for Physico-chemical and optoelectronicproperties, by XRD, XPS, SEM, TEM, UV–Visible DRS, BET, PL, and EIS. The fabricated g-C3N4/Ni3(VO4)2/ZnCr2O4 has shown excellent photocatalytic activity. The complete mineralization of both p-CP and 5-FU observed after 160 and 200 min of visible light irradiation respectively. The mineralizationof p-CP and 5-FU was confirmed by total organic carbon (TOC) estimation and the percentage of removalTOC for p-CP and 5-FU was 99.25% and 98.9% respectively. The stability of the particle was confirmed bysix cycles test. The reusable efficiency of the NCs was found to be 99.7% after six consequent cycles. Thestability of the NCs was confirmed by XRD and XPS analysis of reused photocatalyst. The scavengers assayand ESR analysis confirmed the major role of OH radicals in enhanced photocatalytic activity. The degradationpathway of p-CP and 5-FU was determined by GC–MS/MS and the possible toxicity of the intermediatecompounds was determined by the ECOSAR program, which shows the non-toxic nature ofthe end product on green algae, daphnia, and fish. The toxicity of the NCs was tested against Allium cepawhich further confirm the non-toxic nature of NCs. The study suggests that fabricated g-C3N4/Ni3(VO4)2/ZnCr2O4 NCs can be utilized for environmental remediation applications.

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        ZEITLUPE Contributes to a Thermoresponsive Protein Quality Control System in Arabidopsis

        Gil, Kyung-Eun,Kim, Woe-Yeon,Lee, Hyo-Jun,Faisal, Mohammad,Saquib, Quaiser,Alatar, Abdulrahman A.,Park, Chung-Mo Americ 2017 The Plant cell Vol.29 No.11

        <P>The E3 ligase ZEITLUPE mediates the clearance of denatured protein aggregates under heat stress conditions, thereby enhancing thermotolerance and the thermal stability of the circadian clock.</P><P>Cellular proteins undergo denaturation and oxidative damage under heat stress, forming insoluble aggregates that are toxic to cells. Plants possess versatile mechanisms to deal with insoluble protein aggregates. Denatured proteins are either renatured to their native conformations or removed from cellular compartments; these processes are often referred to as protein quality control. Heat shock proteins (HSPs) act as molecular chaperones that assist in the renaturation-degradation process. However, how protein aggregates are cleared from cells in plants is largely unknown. Here, we demonstrate that heat-induced protein aggregates are removed by a protein quality control system that includes the ZEITLUPE (ZTL) E3 ubiquitin ligase, a central circadian clock component in <I>Arabidopsis thaliana</I>. ZTL mediates the polyubiquitination of aggregated proteins, which leads to proteasomal degradation and enhances the thermotolerance of plants growing at high temperatures. The ZTL-defective <I>ztl-105</I> mutant exhibited reduced thermotolerance, which was accompanied by a decline in polyubiquitination but an increase in protein aggregate formation. ZTL and its interacting partner HSP90 were cofractionated with insoluble aggregates under heat stress, indicating that ZTL contributes to the thermoresponsive protein quality control machinery. Notably, the circadian clock was hypersensitive to heat in <I>ztl-105</I>. We propose that ZTL-mediated protein quality control contributes to the thermal stability of the circadian clock.</P>

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