A5014469167- Microbial bioremediation and biosurfactants
- Enzyme Catalysis and Immobilization
- bioluminescence and chemiluminescence research
- Microbial Metabolic Engineering and Bioproduction
- Amino Acid Enzymes and Metabolism
- Pharmaceutical and Antibiotic Environmental Impacts
- Metal-Catalyzed Oxygenation Mechanisms
- Pesticide and Herbicide Environmental Studies
- Electrochemical sensors and biosensors
- Smoking Behavior and Cessation
- Folate and B Vitamins Research
- Photoreceptor and optogenetics research
- Advanced oxidation water treatment
- Enzyme-mediated dye degradation
- Gout, Hyperuricemia, Uric Acid
- 3D Printing in Biomedical Research
- Innovative Microfluidic and Catalytic Techniques Innovation
- Natural Antidiabetic Agents Studies
- Biochemical and biochemical processes
- Trypanosoma species research and implications
- Mangiferin and Mango Extracts
- Cholinesterase and Neurodegenerative Diseases
- Nicotinic Acetylcholine Receptors Study
- Cell Image Analysis Techniques
- Free Radicals and Antioxidants
Kasetsart University
2020-2024
Silpakorn University
2019-2020
Vidyasirimedhi Institute of Science and Technology
2018-2019
Mahidol University
2017-2018
Enzymes that are capable of detoxifying halogenated phenols (HPs) and nitrophenols (NPs) valuable for bioremediation waste biorefining.
Abstract HadA is a flavin‐dependent monooxygenase that can catalyze the denitration and dehalogenation of wide variety toxicants such as pesticides. Although these enzymatic reactions are useful for bioremediation or biocatalysis, application purposes not yet possible because its low thermostability. In this work we have engineered to be more thermostable through use structural, in silico, rational approaches. The X‐ray structure was solved obtain reliable three‐dimensional protein model...
Halogenated phenol and nitrophenols are toxic compounds that widely accumulated in the environment. Enzymes had operon from bacterium Ralstonia pickettii DTP0602 have potential for application as biocatalysts degradation of many these chemicals. HadA monooxygenase previously was identified a two-component reduced FAD (FADH-)-utilizing with dual activities dehalogenation denitration. However, partner enzymes HadA, is, flavin reductase quinone provide FADH- reduce to hydroquinone, remain be...
Abstract The flavin‐dependent monooxygenase, HadA, catalyzes the dehalogenation and denitration of toxicants, nitro‐ halogenated phenols, to benzoquinone. HadA reaction can be applied in one‐pot reactions towards de novo synthesis d ‐luciferin by coupling with ‐Cys condensation. ‐luciferin, a valuable chemical widely used biomedical applications, as substrate for firefly luciferase generate bioluminescence. As phenols are key indicators human overexposure pesticides pesticide contamination,...
Bacterial luciferase catalyzes a bioluminescent reaction by oxidizing long‐chain aldehydes to acids using reduced FMN and oxygen as co‐substrates. Although flavin C4a‐peroxide anion is postulated be the intermediate reacting with aldehyde prior light liberation, no clear identification of protonation status this has been reported. Here, transient kinetics, pH variation, site‐directed mutagenesis were employed probe state C4a‐hydroperoxide in bacterial luciferase. The first observed...
NAD
The coronavirus (COVID-19) pandemic prevented students from attending on-site classes. Consequently, their face-to-face interactions decreased. Thus, it became crucial to design learning activities enhance the motivation of and inspire them achieve desired outcomes during long disruption Mobile devices applications represent most frequently used alternatives online tools. During COVID-19 pandemic, biochemists faced challenges integrating technology biochemistry principles allow investigate...
HadA is a flavin-dependent monooxygenase catalyzing hydroxylation plus dehalogenation/denitration, which useful for biodetoxification and biodetection. In this study, the X-ray structure of wild-type (HadAWT) co-complexed with reduced FAD (FADH–) 4-nitrophenol (4NP) (HadAWT−FADH–−4NP) was solved at 2.3-Å resolution, providing first full package (with flavin substrate bound) type. Residues Arg101, Gln158, Arg161, Thr193, Asp254, Arg233, Arg439 constitute flavin-binding pocket, whereas...
The dimethyl sulfone monooxygenase system is a two‐component flavoprotein, catalyzing the monooxygenation of (DMSO 2 ) by oxidative cleavage producing methanesulfinate and formaldehyde. reductase component (DMSR) flavoprotein with FMN as cofactor, flavin reduction using NADH. (DMSMO) uses reduced from oxygen for substrate monooxygenation. DMSMO can bind to FMNH − K d 17.4 ± 0.9 μ m 4.08 0.8 , respectively. binding required prior DMSO . This also applies fast followed Substituting DMSR...
Secondhand smoke (SHS) poses the most considerable health risk to children in urban households. However, limited evidence exists regarding impact of exposure SHS on gamma-aminobutyric acid (GABA) levels. This study aimed investigate level cotinine and GABA their association with variables related exposed SHS.
Abstract HadA monooxygenase is involved in the initial step of biodegradation pathway toxic nitrophenols and halogenated phenols. catalyzes O 2 ‐dependent denitration dehalogenation phenols via hydroquinone pathway. Based on bioinformatics structural analysis, Arg208 located at proper position for substrate stabilization. This arginine conserved among pathway‐specific enzymes toxicant detoxification. In this study, function was determined by a single‐point mutation creating variants....
Succinic semialdehyde dehydrogenase (SSADH) catalyses the conversion of succinic into acid and two electrons are transferred to NAD(P) + yield NAD(P)H. Our previous work has already reported catalytic role Cys289 two‐cysteine SSADH from Acinetobacter baumannii ( Ab SSADH). However, mechanistic neighbouring conserved Cys291 Glu255 remains unexplored. In this study, functional roles in catalysis have been characterized. Results demonstrated that E255A activity was almost completely lost, ~...
1. World Health Organization. WHO report on the global tobacco epidemic, 2017: Monitoring use and prevention policies. WHO; 2017. Accessed March 12, 2024. https://www.who.int/publicatio... Google Scholar
Abstract The flavin‐dependent monooxygenase, HadA, catalyzes the dehalogenation and denitration of toxicants, nitro‐ halogenated phenols, to benzoquinone. HadA reaction can be applied in one‐pot reactions towards de novo synthesis d ‐luciferin by coupling with ‐Cys condensation. ‐luciferin, a valuable chemical widely used biomedical applications, as substrate for firefly luciferase generate bioluminescence. As phenols are key indicators human overexposure pesticides pesticide contamination,...
HadA monooxygenase catalyses the detoxification of halogenated phenols and nitrophenols via dehalogenation denitration respectively. C4a-hydroperoxy-FAD is a key reactive intermediate wherein its formation, protonation stabilization reflect enzyme efficiency. Herein, transient kinetics, site-directed mutagenesis pH-dependent behaviours reaction were employed to identify features stabilizing C4a-adducts in HadA. The formation pH independent, whereas decay distal oxygen are associated with pKa...