Propiconazole (PCZ) is a hepatotoxic triazole fungicide. There are insufficient data on how PCZ induces liver fibrosis in humans. This study aimed to investigate the effect of PCZ on liver fibrosis and its underlying mechanisms. HepG2 cells and Sprague-Dawley rats were exposed to PCZ at doses of 0-160 μM (3-72 h) and 0.5-50 mg/kg body weight/day (28 days), respectively. PCZ-treated cells activated intracellular oxidative stress via cytochrome P450 and had higher mRNA levels of interleukin-1β, tumor necrosis factor-α, matrix metalloproteinase (MMP)-2, MMP-9, and transforming growth factor-β (TGF-β) than the control. PCZ treatment in cells induced a morphological transition with E-cadherin decrease and vimentin and Snail increase via the oxidative stress and TGF-β/Smad pathways. PCZ administration in rats induced liver fibrosis through pathological changes, epithelial-mesenchymal transition, and collagen deposition. Thus, our data suggest that exposure of PCZ to humans may be a risk factor for the functional integrity of the liver.Recent DFT based molecular engineering to obtain stable oxathiirane S-oxide derivatives evokes the recommencement of the use of carbenes for the sequestering of SO2, which has been kept separate so far. Carbene is one of the key chemicals for the sequestering of various premier greenhouse gases like CO2, CO, N2O, etc. In this respect, a comparative study of the reactivity of carbenes with variant greenhouse gases is highly demanding.  https://www.selleckchem.com/products/fl118.html  The present investigation is engrossed in the comparative reactivity of SO2 and NO2 with carbenes. All three selected carbenes are highly susceptible to SO2 and NO2. Through an immaculate mechanistic study, we are able to corroborate that the end product of the carbene-SO2 reaction is an adduct which has a preferable structure having a six-membered ring with hydrogen bonding instead of ketone and SO with higher thermodynamic stability than the corresponding oxathiirane S-oxide derivative. Carbene reacts with NO2 to form a stable carbene N, N-dioxide derivative which forms vibrationally excited oxaziridine N-oxide which rapidly dissociates to form a ketone derivative. The formation of carbene S, S-dioxide and carbene N, N-dioxide is a barrierless process. The dissociation of oxaziridene N-oxide is also a barrierless process.Water contamination is a global threat due to its damaging effects on the environment and human health. Water pollution by microplastics (MPs), dissolved natural organic matter (NOM), and other turbid particles is ubiquitous in water treatment. Here, we introduce lysozyme amyloid fibrils as a novel natural bio-flocculant and explore their ability to flocculate and precipitate the abovementioned undesired colloidal objects. Thanks to their positively charged surface in a very broad range of pH, lysozyme amyloid fibrils show an excellent turbidity removal efficiency of 98.2 and 97.9% for dispersed polystyrene MPs and humic acid (HA), respectively. Additionally, total organic carbon measurements confirm these results by exhibiting removal efficiencies of 93.4 and 61.9% for purifying water from dispersed MPs and dissolved HA, respectively. The comparison among amyloid fibrils, commercial flocculants (FeCl3 and polyaluminumchloride), and native lysozyme monomers points to the superiority of amyloid fibrils at the same dosage and sedimentation time. Furthermore, the turbidity of pristine and MP-spiked wastewater and lake water decreased after the treatment by amyloid fibrils, validating their coagulation-flocculation performance under natural conditions. All these results demonstrate lysozyme amyloid fibrils as an appropriate natural bio-flocculant for removing dispersed MPs, NOM, and turbid particles from water.Perfluoroalkyl carboxylic acids (PFCAs) are ubiquitous contaminants known for their bioaccumulation, toxicological harm, and resistance to degradation. Remediating PFCAs in water is an ongoing challenge with existing technologies being insufficient or requiring additional disposal. An emergent approach is using activated persulfate, which degrades PFCAs through sequential scission of CF2 equivalents yielding shorter-chain homologues, CO2 and F-. This transformation is thought to be initiated by single electron transfer (SET) from the PFCA to the activate oxidant, SO4•-. A pronounced pH effect has been observed for thermally activated persulfate PFCA transformation. To evaluate the role of pH during SET, we directly determined absolute rate constants for perfluorobutanoic acid and trifluoroacetic acid oxidation by SO4•- in the pH range of 0.5-4.0 using laser flash photolysis. The average of the rate constants for both substrates across all pH values was 9 ± 2 × 103 M-1 s-1 (±2σ), implying that acid catalysis of thermal persulfate activation may be the primary culprit of the observed pH effect, instead of pH influencing the SET step. In addition, density functional theory was used to investigate if SO4•-protonation might enhance PFCA transformation kinetics. We found that when calculations include explicit water molecules, direct SO4•- protonation does not occur.The particulate methane monooxygenase (pMMO) is the first enzyme in the C1 metabolic pathway in methanotrophic bacteria. As this enzyme converts methane into methanol efficiently near room temperature, it has become the paradigm for developing an understanding of this difficult C1 chemistry. pMMO is a membrane-bound protein with three subunits (PmoB, PmoA, and PmoC) and 12-14 coppers distributed among different sites. X-ray crystal structures that have revealed only three mononuclear coppers at three sites have neither disclosed the location of the active site nor the catalytic mechanism of the enzyme. Here we report a cyro-EM structure of holo-pMMO from Methylococcus capsulatus (Bath) at 2.5 Å, and develop quantitative electrostatic-potential profiling to scrutinize the nonprotein densities for signatures of the copper cofactors. Our results confirm a mononuclear CuI at the A site, resolve two CuIs at the B site, and uncover additional CuI clusters at the PmoA/PmoC interface within the membrane (D site) and in the water-exposed C-terminal subdomain of the PmoB (E clusters).