scholarly journals Early Chemistry of Nicotine Degradation in Heat-Not-Burn Smoking Devices and Conventional Cigarettes: Implications for Users and Second- and Third-Hand Smokers

2021 ◽  
Author(s):  
Javier E. Chavarrio Cañas ◽  
M. Monge-Palacios ◽  
E. Grajales-González ◽  
S. Mani Sarathy
Keyword(s):  
Nicotine Degradation

scholarly journals Characterization of Pseudooxynicotine Amine Oxidase of Pseudomonas putida S16 that Is Crucial for Nicotine Degradation

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Haiyang Hu ◽  
Weiwei Wang ◽  
Hongzhi Tang ◽  
Ping Xu
Keyword(s):  
Pseudomonas Putida ◽  
Amine Oxidase ◽  
Nicotine Degradation

Nicotine degradation by two novel bacterial isolates of Acinetobacter sp. TW and Sphingomonas sp. TY and their responses in the presence of neonicotinoid insecticides

2010 ◽  
Vol 27 (7) ◽  
pp. 1633-1640 ◽  
Author(s):  
Meizhen Wang ◽  
Guiqin Yang ◽  
Xin Wang ◽  
Yanlai Yao ◽  
Hang Min ◽  
...  
Keyword(s):  
Bacterial Isolates ◽  
Neonicotinoid Insecticides ◽  
Nicotine Degradation ◽  
Acinetobacter Sp

scholarly journals Effect of Transient Nicotine Load Shock on the Performance ofPseudomonassp. HF-1 Bioaugmented Sequencing Batch Reactors

2016 ◽  
Vol 2016 ◽  
pp. 1-8
Author(s):  
Dong-sheng Shen ◽  
Li-jia Wang ◽  
Hong-zhen He ◽  
Mei-zhen Wang
Keyword(s):  
Oxidative Stress ◽  
Industrial Wastewater ◽  
Control Level ◽  
Batch Reactors ◽  
Sequencing Batch Reactors ◽  
Shock Loads ◽  
Toc Removal ◽  
Degrading Bacteria ◽  
Nicotine Degradation ◽  
Tobacco Waste

Bioaugmentation with degrading bacteria can improve the treatment of nicotine-containing tobacco industrial wastewater effectively. However, the transient and extremely high feeding of pollutants may compromise the effectiveness of the bioaugmented reactors. The effect of transient nicotine shock loads on the performance ofPseudomonassp. HF-1 bioaugmented SBRs were studied. The results showed that, under 500–2500 mg/L of transient nicotine shocks, all the reactors still could realize 100% of nicotine degradation in 4 days of recovery, while the key nicotine degradation enzyme HSP hydroxylase increased in expression. Though the dramatic increase of activities of ROS, MDA, SOD, and CAT suggested that transient nicotine shock loads could induce oxidative stress on microorganisms in activated sludge, a decrease to control level demonstrated that most of the microorganisms could resist 500–1500 mg/L of transient nicotine shock under the protection from strain HF-1. After 8 cycles of recovery, high ROS level and low TOC removal in high transient shock reactors implied that 2000–2500 mg/L of transient nicotine shock was out of its recovery of strain HF-1 bioaugmented system. This study enriched our understanding on highly efficient nicotine-degrading strain bioaugmented system, which would be beneficial to tobacco waste or wastewater treatment in engineering.

A novel pathway for nicotine degradation by Aspergillus oryzae 112822 isolated from tobacco leaves

2010 ◽  
Vol 161 (7) ◽  
pp. 626-633 ◽  
Author(s):  
Xiang Jing Meng ◽  
Li Li Lu ◽  
Guo Feng Gu ◽  
Min Xiao
Keyword(s):  
Aspergillus Oryzae ◽  
Tobacco Leaves ◽  
Nicotine Degradation

scholarly journals Cloning of a Novel Nicotine Oxidase Gene from Pseudomonas sp. Strain HZN6 Whose Product Nonenantioselectively Degrades Nicotine to Pseudooxynicotine

2013 ◽  
Vol 79 (7) ◽  
pp. 2164-2171 ◽  
Author(s):  
Jiguo Qiu ◽  
Yun Ma ◽  
Jing Zhang ◽  
Yuezhong Wen ◽  
Weiping Liu
Keyword(s):  
Amine Oxidase ◽  
Sole Source ◽  
Site Directed Mutagenesis ◽  
Broad Host Range ◽  
Upstream Sequence ◽  
Oxidase Gene ◽  
Content Type ◽  
Reading Frame ◽  
Degrading Bacteria ◽  
Nicotine Degradation

ABSTRACTPseudomonassp. strain HZN6 utilizes nicotine as its sole source of carbon, nitrogen, and energy. However, its catabolic mechanism has not been elucidated. In this study, self-formed adaptor PCR was performed to amplify the upstream sequence of the pseudooxynicotine amine oxidase gene. A 1,437-bp open reading frame (designatednox) was found to encode a nicotine oxidase (NOX) that shows 30% amino acid sequence identity with 6-hydroxy-l-nicotine oxidase fromArthrobacter nicotinovorans. Thenoxgene was cloned into a broad-host-range cloning vector and transferred into the non-nicotine-degrading bacteriaEscherichia coliDH5α (DH-nox) andPseudomonas putidaKT2440 (KT-nox). The transconjugant KT-nox obtained nicotine degradation ability and yielded an equimolar amount of pseudooxynicotine, while DH-nox did not. Reverse transcription-PCR showed that thenoxgene is expressed in both DH5α and KT2440, suggesting that additional factors required for nicotine degradation are present in aPseudomonasstrain(s), but not inE. coli. The mutant of strain HZN6 withnoxdisrupted lost the ability to degrade nicotine, but not pseudooxynicotine. These results suggested that thenoxgene is responsible for the first step of nicotine degradation. The (RS)-nicotine degradation results showed that the two enantiomers were degraded at approximately the same rate, indicating that NOX does not show chiral selectivity. Site-directed mutagenesis revealed that both the conserved flavin adenine dinucleotide (FAD)-binding GXGXXG motif and His456 are essential for nicotine degradation activity.

scholarly journals 6-Hydroxypseudooxynicotine Dehydrogenase Delivers Electrons to Electron Transfer Flavoprotein during Nicotine Degradation by Agrobacterium tumefaciens S33

2019 ◽  
Vol 85 (11) ◽  
Author(s):  
Rongshui Wang ◽  
Jihong Yi ◽  
Jinmeng Shang ◽  
Wenjun Yu ◽  
Zhifeng Li ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Agrobacterium Tumefaciens ◽  
Electron Transport ◽  
Electron Acceptor ◽  
Aromatic Compounds ◽  
Coenzyme Q ◽  
Content Type ◽  
Electron Transfer Flavoprotein ◽  
Nicotine Degradation

ABSTRACT Agrobacterium tumefaciens S33 degrades nicotine via a novel hybrid of the pyridine and the pyrrolidine pathways. The hybrid pathway consists of at least six steps involved in oxidoreductive reactions before the N-heterocycle can be broken down. Collectively, the six steps allow electron transfer from nicotine and its intermediates to the final acceptor O2 via the electron transport chain (ETC). 6-Hydroxypseudooxynicotine oxidase, renamed 6-hydroxypseudooxynicotine dehydrogenase in this study, has been characterized as catalyzing the fourth step using the artificial electron acceptor 2,6-dichlorophenolindophenol. Here, we used biochemical, genetic, and liquid chromatography-mass spectrometry (LC-MS) analyses to determine that 6-hydroxypseudooxynicotine dehydrogenase utilizes the electron transfer flavoprotein (EtfAB) as the physiological electron acceptor to catalyze the dehydrogenation of pseudooxynicotine, an analogue of the true substrate 6-hydroxypseudooxynicotine, in vivo, into 3-succinoyl-semialdehyde-pyridine. NAD(P)+, O2, and ferredoxin could not function as electron acceptors. The oxygen atom in the aldehyde group of the product 3-succinoyl-semialdehyde-pyridine was verified to be derived from H2O. Disruption of the etfAB genes in the nicotine-degrading gene cluster decreased the growth rate of A. tumefaciens S33 on nicotine but not on 6-hydroxy-3-succinoylpyridine, an intermediate downstream of the hybrid pathway, indicating the requirement of EtfAB for efficient nicotine degradation. The electrons were found to be further transferred from the reduced EtfAB to coenzyme Q by the catalysis of electron transfer flavoprotein:ubiquinone oxidoreductase. These results aid in an in-depth understanding of the electron transfer process and energy metabolism involved in the nicotine oxidation and provide novel insights into nicotine catabolism in bacteria. IMPORTANCE Nicotine has been studied as a model for toxic N-heterocyclic aromatic compounds. Microorganisms can catabolize nicotine via various pathways and conserve energy from its oxidation. Although several oxidoreductases have been characterized to participate in nicotine degradation, the electron transfer involved in these processes is poorly understood. In this study, we found that 6-hydroxypseudooxynicotine dehydrogenase, a key enzyme in the hybrid pyridine and pyrrolidine pathway for nicotine degradation in Agrobacterium tumefaciens S33, utilizes EtfAB as a physiological electron acceptor. Catalyzed by the membrane-associated electron transfer flavoprotein:ubiquinone oxidoreductase, the electrons are transferred from the reduced EtfAB to coenzyme Q, which then could enter into the classic ETC. Thus, the route for electron transport from the substrate to O2 could be constructed, by which ATP can be further sythesized via chemiosmosis to support the baterial growth. These findings provide new knowledge regarding the catabolism of N-heterocyclic aromatic compounds in microorganisms.

Impacts of configurations of the up-flow anaerobic sludge blanket reactor and nitrogen forms on the nicotine degradation in tobacco sheet wastewater

2017 ◽  
Vol 79 ◽  
pp. 49-55
Author(s):  
Aidong Ruan ◽  
Chenxiao Liu ◽  
Weiheng Wu ◽  
Chao Fang
Keyword(s):  
Anaerobic Sludge ◽  
Nitrogen Forms ◽  
Nicotine Degradation ◽  
Anaerobic Sludge Blanket

scholarly journals Periplasmic Nicotine Dehydrogenase NdhAB Utilizes Pseudoazurin as Its Physiological Electron Acceptor in Agrobacterium tumefaciens S33

2017 ◽  
Vol 83 (17) ◽  
Author(s):  
Wenjun Yu ◽  
Rongshui Wang ◽  
Haiyan Huang ◽  
Huijun Xie ◽  
Shuning Wang
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Signal Peptide ◽  
Electron Acceptor ◽  
Initial Step ◽  
Hydroxyl Group ◽  
Specific Rate ◽  
Periplasmic Space ◽  
Electron Carrier ◽  
Content Type ◽  
Nicotine Degradation

ABSTRACT Agrobacterium tumefaciens S33 can grow with nicotine as the sole source of carbon, nitrogen, and energy via a novel hybrid of the pyridine pathway and the pyrrolidine pathway. Characterization of the enzymes involved in the hybrid pathway is important for understanding its biochemical mechanism. Here, we report that the molybdenum-containing nicotine dehydrogenase (NdhAB), which catalyzes the initial step of nicotine degradation, is located in the periplasm of strain S33, while the 6-hydroxynicotine oxidase and 6-hydroxypseudooxynicoine oxidase are in the cytoplasm. This is consistent with the fact that NdhA has a Tat signal peptide. Interestingly, an open reading frame (ORF) adjacent to the ndhAB gene was verified to encode a copper-containing electron carrier, pseudoazurin (Paz), which has a signal peptide typical of bacterial Paz proteins. Both were transported into the periplasm after being produced in the cytoplasm. We purified NdhAB from the periplasmic fraction of strain S33 and found that with Paz as the physiological electron acceptor, NdhAB catalyzed the hydroxylation of nicotine at a specific rate of 110.52 ± 8.09 μmol · min−1 · mg of protein−1, where the oxygen atom in the hydroxyl group of the product 6-hydroxynicotine was derived from H2O. The apparent Km values for nicotine and Paz were 1.64 ± 0.07 μM and 3.61 ± 0.23 μM, respectively. NAD(P)+, O2, and ferredoxin could not serve as electron acceptors. Disruption of the paz gene disabled the strain for nicotine degradation, indicating that Paz is required for nicotine catabolism in the strain. These findings help our understanding of electron transfer during nicotine degradation in bacteria. IMPORTANCE Nicotine is a toxic and addictive N-heterocyclic aromatic alkaloid produced in tobacco. Its catabolism in organisms and degradation in tobacco wastes have become major concerns for human health and the environment. Bacteria usually decompose nicotine using the classical strategy of hydroxylating the pyridine ring with the help of activated oxygen by nicotine dehydrogenase, which binds one molybdopterin, two [2Fe2S] clusters, and usually one flavin adenine dinucleotide (FAD) as well. However, the physiological electron acceptor for the reaction is still unknown. In this study, we found that the two-component nicotine dehydrogenase from Agrobacterium tumefaciens S33, naturally lacking an FAD-binding domain, is located in the periplasmic space and uses a copper-containing electron carrier, pseudoazurin, as its physiological electron acceptor. We report here the role of pseudoazurin in a reaction catalyzed by a molybdopterin-containing hydroxylase occurring in the periplasmic space. These results provide new biochemical knowledge on microbial degradation of N-heterocyclic aromatic compounds.

Nicotine Degradation in vitro induced by Agents from Tobacco Seed

Nature ◽  
1955 ◽  
Vol 175 (4465) ◽  
pp. 945-946 ◽  
Author(s):  
WALTER G. FRANKENBURG
Keyword(s):  
Tobacco Seed ◽  
Nicotine Degradation

scholarly journals Dysregulated Metabolites Serve as Novel Biomarkers for Metabolic Diseases Caused by Vaping and Cigarette Smoking

2021 ◽  
Author(s):  
Qixin Wang ◽  
Xianming Ji ◽  
Irfan Rahman
Keyword(s):  
Cigarette Smoking ◽  
Cigarette Smoke ◽  
Metabolic Diseases ◽  
Tca Cycle ◽  
Limited Information ◽  
Cigarette Smokers ◽  
Metabolic Signature ◽  
Nicotine Degradation ◽  
Different Types ◽  
Novel Biomarkers

Metabolites are essential intermediate products in metabolism, and metabolism dysregulation indicates different types of diseases. Previous studies have shown that cigarette smoke dysregulated metabolites; however, limited information is available with electronic cigarette (E-cig) vaping. We hypothesized that E-cig vaping and cigarette smoking altered systemic metabolites, and we propose to understand the specific metabolic signature between E-cig users and cigarette smokers. Plasma from non-smoker controls, cigarette smokers, and e-cig users were collected, and metabolites were identified by UPLC–MS (Ultraperformance liquid chromatography-mass spectrometer). Nicotine degradation was activated by e-cig vaping and cigarette smoking with increased concentrations of cotinine, cotinine N-oxide, (S)-nicotine, and (R)-6-hydroxynicotine. Additionly, we found significant decreased concentrations in metabolites associated with tricarboxylic acid (TCA) cycle pathways in e-cig users verses cigarette smokers, such as: D-glucose, (2R,3S)-2,3-dimethylmalate, (R)-2-hydroxyglutarate, O-phosphoethanolamine, malathion, D-threo-isocitrate, malic acid, and 4-acetamidobutanoic acid. Cigarette smoking significant up-regulated sphingolipid metabolites, such as D-sphingosine, ceramide, N-(octadecanoyl)-sphing-4-enine, N-(9Z-octadecenoyl)-sphing-4-enine, and N-[(13Z)-docosenoyl]sphingosine, verses e-cig vaping. Overall, e-cig vaping dysregulated TCA cycle realted metabolites while cigarette smoking altered sphingolipid metabolites. Both e-cig and cigarette smoke increased nicotinic metabolites. Therefore, specific metabolic signature altered by e-cig vaping and cigarette smoking could serve as potential systemic biomarkers for early cardiopulmonary diseases.

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