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In this work, two novel luminescent molecules containing distorted phenothiazine-S-oxide and phenothiazine-S,S dioxide skeletons were synthesized by oxidation reactions using different oxidants (m-chloroperoxybenzoic acid, acetic acid /hydrogen peroxide). The target compounds were all confirmed by H NMR, C NMR and EI-MS. Combined with the results of UV-vis absorption spectra and fluorescence emission spectra, we found that the different oxidation states of S-atom, from sulfide (+2) to sulfoxide (+4) and sulfone (+6), led to the blue, yellow-green and yellowish fluorescence of these compounds in the solid states. Subsequent studies showed that the molecule containing the phenothiazine-S-oxide skeleton exhibited obvious solvatochromism, and the increase of solvent polarity induced a red-shift in the emission wavelength. Moreover, this molecule also exhibited a rare self-recovery mechanochromatic behavior. In addition, these properties were further confirmed by theoretical calculations and X-ray single-crystal diffraction analysis.
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http://dx.doi.org/10.1016/j.saa.2023.122427 | DOI Listing |
Arch Med Res
September 2025
Department and Graduate Institute of Microbiology and Immunology, National Defense Medical Center, Taipei, Taiwan. Electronic address:
Background: Atherosclerosis, a leading cause of cardiovascular disease (CVD) mortality worldwide, is characterized by dysregulated lipid metabolism and unresolved inflammation. Macrophage-derived foam cell formation and apoptosis contribute to plaque formation and vulnerability. Elevated serum galectin-3 (Gal-3) levels are associated with increased CVD risk, and Gal-3 in plaques is strongly associated with macrophages.
View Article and Find Full Text PDFLangmuir
September 2025
Laboratory of Electrochemistry-Corrosion, Metallurgy and Inorganic Chemistry, Faculty of Chemistry, USTHB, BP 32, 16111, Algiers, Algeria.
Azo dyes, prevalent in various industries, including textile dyeing, food, and cosmetics, pose significant environmental and health risks due to their chemical stability and toxicity. This study introduces the synthesis and application of a copper hydrogen-π-bonded benzoate framework (Cu-HBF) and its derived marigold flower-like copper oxide (MFL-CuO) in a synergetic adsorption-photocatalytic process for efficiently removing cationic azo dyes from water, specifically crystal violet (CV), methylene blue (MB), and rhodamine B (RhB). The Cu-HBF, previously available only in single crystal form, is prepared here as a crystalline powder for the first time, using a low-cost and facile procedure, allowing its application as an adsorbent and also serving as a precursor for synthesizing well-structured copper oxide (MFL-CuO).
View Article and Find Full Text PDFJ Am Chem Soc
September 2025
National Engineering Research Center of Lower-Carbon Catalysis Technology, Dalian National Laboratory for Clean Energy, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Zeolite-confined Rh-based catalysts have emerged as promising heterogeneous candidates for olefin hydroformylation. However, they face challenges of reactant- and product-induced Rh leaching and aggregation. Herein, zeolite framework-anchored Rh-(O-Zn) sites were designed and are shown to have remarkable activity and stability for gas-phase ethylene hydroformylation.
View Article and Find Full Text PDFInorg Chem
September 2025
State Key Laboratory of Inorganic Synthesis and Preparative Chemistry, College of Chemistry, Jilin University, Changchun 130021, P. R. China.
The CO cycloaddition route is an effective way to achieve efficient conversion and utilization of CO. Zeolites with diverse topologies and tunable acidic sites can efficiently promote the cycloaddition reaction of CO with epoxides. The exchangeable cations in zeolites have a great influence on the performance of the CO cycloaddition, but there are few studies on it.
View Article and Find Full Text PDFJ Agric Food Chem
September 2025
College of Plant Protection, Northwest A&F University, Yangling, Shaanxi 712100, China.
Protoporphyrinogen oxidase (PPO, EC 1.3.3.
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