“…Levels of biotin carboxylase, a subunit of acetyl-CoA carboxylase involved in both fatty acid and pyruvate biosynthesis, are augmented in iTRAQ results (Supplementary Table S5 ). A previous study 4 suggests that the limitation of fatty acid synthesis by TPT signifies that biotin carboxylase is associated with gluconeogenesis (Fig. 5b ).…”
Section: Resultsmentioning
confidence: 72%
“…4a ). These findings explained why TPT suppresses fatty acid synthesis 4 . Figure 4 Analysis of effector proteins with same expression trends in different experiments.…”
Section: Resultsmentioning
confidence: 82%
“…4a). These findings explained why TPT suppresses fatty acid synthesis 4 .Figure 4Analysis of effector proteins with same expression trends in different experiments. ( a ) protein network of electron transfer flavoprotein subunit alpha (medium confidence: 0.400); ( b ) homology analysis of different species.
…”
Section: Resultsmentioning
confidence: 90%
“…Biodegradation is a primary approach used to reduce TPT and its derivatives in a natural environment without exposure to ultraviolet radiation. Regarding the effective microbes for TPT degradation, Bacillus thuringiensis can effectively cleave the carbon-tin bonds of organotins and degrade organotins 4 , 5 . This spore-forming species was selected in the current study due to its use as a commonly used biopesticide without negative impacts on humans, wildlife, and pollinators 6 ; its TPT degradation ability; and its resistance to a variety of stresses, including pollutant toxicity.…”
Section: Introductionmentioning
confidence: 99%
“…This spore-forming species was selected in the current study due to its use as a commonly used biopesticide without negative impacts on humans, wildlife, and pollinators 6 ; its TPT degradation ability; and its resistance to a variety of stresses, including pollutant toxicity. Metabolite analysis has revealed that TPT is degraded by B. thuringiensis through the successive dephenylation pathway, producing diphenyltin, monophenyltin and tin 4 . This process has been associated with the metabolism of ions, carbohydrates and organic acids 7 and is regulated by cellular protein networks.…”
Herein, triphenyltin (TPT) biodegradation efficiency and its transformation pathway have been elucidated. To better understand the molecular mechanism of TPT degradation, the interactions between amino acids, primary structures, and quaternary conformations of effector proteins and TPT were studied. The results verified that TPT recognition and binding depended on amino acid sequences but not on secondary, tertiary or quaternary protein structure. During this process, TPT could change the molecular weight and isoelectric point of effector proteins, induce their methylation or demethylation, and alter their conformation. The effector proteins, alkyl hydroperoxide reductase and acetyl-CoA acetyltransferase, recognizing TPT were crucial to TPT degradation. Electron transfer flavoprotein subunit alpha, phosphoenolpyruvate carboxykinase, aconitate hydratase, branched-chain alpha-keto acid dehydrogenase E1 component, biotin carboxylase and superoxide dismutase were related to energy and carbon metabolism, which was consistent with the results in vivo. The current findings develop a new approach for investigating the interactions between proteins and target compounds.
“…Levels of biotin carboxylase, a subunit of acetyl-CoA carboxylase involved in both fatty acid and pyruvate biosynthesis, are augmented in iTRAQ results (Supplementary Table S5 ). A previous study 4 suggests that the limitation of fatty acid synthesis by TPT signifies that biotin carboxylase is associated with gluconeogenesis (Fig. 5b ).…”
Section: Resultsmentioning
confidence: 72%
“…4a ). These findings explained why TPT suppresses fatty acid synthesis 4 . Figure 4 Analysis of effector proteins with same expression trends in different experiments.…”
Section: Resultsmentioning
confidence: 82%
“…4a). These findings explained why TPT suppresses fatty acid synthesis 4 .Figure 4Analysis of effector proteins with same expression trends in different experiments. ( a ) protein network of electron transfer flavoprotein subunit alpha (medium confidence: 0.400); ( b ) homology analysis of different species.
…”
Section: Resultsmentioning
confidence: 90%
“…Biodegradation is a primary approach used to reduce TPT and its derivatives in a natural environment without exposure to ultraviolet radiation. Regarding the effective microbes for TPT degradation, Bacillus thuringiensis can effectively cleave the carbon-tin bonds of organotins and degrade organotins 4 , 5 . This spore-forming species was selected in the current study due to its use as a commonly used biopesticide without negative impacts on humans, wildlife, and pollinators 6 ; its TPT degradation ability; and its resistance to a variety of stresses, including pollutant toxicity.…”
Section: Introductionmentioning
confidence: 99%
“…This spore-forming species was selected in the current study due to its use as a commonly used biopesticide without negative impacts on humans, wildlife, and pollinators 6 ; its TPT degradation ability; and its resistance to a variety of stresses, including pollutant toxicity. Metabolite analysis has revealed that TPT is degraded by B. thuringiensis through the successive dephenylation pathway, producing diphenyltin, monophenyltin and tin 4 . This process has been associated with the metabolism of ions, carbohydrates and organic acids 7 and is regulated by cellular protein networks.…”
Herein, triphenyltin (TPT) biodegradation efficiency and its transformation pathway have been elucidated. To better understand the molecular mechanism of TPT degradation, the interactions between amino acids, primary structures, and quaternary conformations of effector proteins and TPT were studied. The results verified that TPT recognition and binding depended on amino acid sequences but not on secondary, tertiary or quaternary protein structure. During this process, TPT could change the molecular weight and isoelectric point of effector proteins, induce their methylation or demethylation, and alter their conformation. The effector proteins, alkyl hydroperoxide reductase and acetyl-CoA acetyltransferase, recognizing TPT were crucial to TPT degradation. Electron transfer flavoprotein subunit alpha, phosphoenolpyruvate carboxykinase, aconitate hydratase, branched-chain alpha-keto acid dehydrogenase E1 component, biotin carboxylase and superoxide dismutase were related to energy and carbon metabolism, which was consistent with the results in vivo. The current findings develop a new approach for investigating the interactions between proteins and target compounds.
Although the degradation of cyanotoxins by 254 nm UV/HO has been well elucidated, the efficiency and mechanism involved are not necessarily true for other UV wavelengths. The degradation of microcystin-LR (MC-LR), a representative cyanotoxin, was explored by UV/HO using 265 nm ultraviolet light-emitting diode (UV-LED). The results indicated that 265 nm UV/HO treatment had a high removal efficiency of MC-LR ([MC-LR] = 0.1 μM, apparent rate constants reached 0.2077 min, half-time at 3.3 min). The qualitative analyses demonstrated that three novel intermediates, CHNO (molecular weight = 1030.5335), CHNO (854.4134), and CHNO (814.3821), were generated in 265 nm UV/HO. Five published intermediates were also confirmed. The generative pathway of these products mainly involved free hydroxyl radical oxidation, resulting in consecutive hydroxyl substitutions and hydroxyl additions of unsaturated bonds in MC-LR. The toxicity of MC-LR was weaken with a relative low mineralization. The electrical energy per order values were calculated to be in the range of 0.00447 to 0.00612 kWh m order for 100-5000 μg L MC-LR. Overall, 265 nm UV-LED/HO can be used as an alternative effective technology to improve the removal efficiency of MC-LR in water.
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