Search results for "OXIDATION"

showing 10 items of 1913 documents

Growth of Rhodococcus sp. strain BCP1 on gaseous n-alkanes: New metabolic insights and transcriptional analysis of two soluble di-iron monooxygenase …

2015

none 7 si Rhodococcus sp. strain BCP1 was initially isolated for its ability to grow on gaseous n-alkanes, which act as inducers for the co-metabolic degradation of low-chlorinated compounds. Here, both molecular and metabolic features of BCP1 cells grown on gaseous and short-chain n-alkanes (up to n-heptane) were examined in detail. We show that propane metabolism generated terminal and sub-terminal oxidation products such as 1- and 2-propanol, whereas 1-butanol was the only terminal oxidation product detected from n-butane metabolism. Two gene clusters, prmABCD and smoABCD—coding for Soluble Di-Iron Monooxgenases (SDIMOs) involved in gaseous n-alkanes oxidation—were detected in the BCP1 g…

Microbiology (medical)Gaseous n-alkaneSoluble di-iron monooxygenaseStrain (chemistry)lcsh:QR1-502Monooxygenase gene expressionMetabolismgaseous n-alkanesMonooxygenaseBiologyLyaseRedoxMicrobiologyPrimer extensionlcsh:MicrobiologyChaperoninRhodococcus sp strain BCP1; soluble di-iron monooxygenase; propane and n-butane oxidation; gaseous n-alkanes; monooxygenase gene expressionBiochemistryRhodococcus sp. strain BCP1Rhodococcus sp strain BCP1Propane and n-butane oxidationGeneOriginal Researchpropane and butane oxidation
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Electron microprobe technique for the determination of iron oxidation state in silicate glasses

2018

We present a new calibration for the determination of the iron oxidation state in silicate glasses by electron probe microanalysis (EPMA) with the "flank method." This method is based on the changes in both intensity and wavelength of the FeLα and FeLβ X-ray emission lines with iron oxidation state. The flank method utilizes the maximum difference for the FeLα and FeLβ spectra observed at the peak flanks between different standard materials, which quantitatively correlates with the Fe2+ content. Provided that this correlation is calibrated on reference materials, the Fe2+/ΣFe ratio can be determined for samples with known total Fe content. Two synthetic Fe-rich ferric and ferrous garnet end…

MicroprobeMaterials science010504 meteorology & atmospheric sciencesInorganic chemistryElectron microprobe010502 geochemistry & geophysics01 natural sciencesRedoxflank methodferric-ferrous ratioGeophysicsGeochemistry and PetrologyOxidation stateredox statepillow glassesSilicate glassMicroprobesilicate glasses0105 earth and related environmental sciences
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Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species

2010

This review highlights the important role of redox signaling between mitochondria and NADPH oxidases. Besides the definition and general importance of redox signaling, the cross-talk between mitochondrial and Nox-derived reactive oxygen species (ROS) is discussed on the basis of 4 different examples. In the first model, angiotensin-II is discussed as a trigger for NADPH oxidase activation with subsequent ROS-dependent opening of mitochondrial ATP-sensitive potassium channels leading to depolarization of mitochondrial membrane potential followed by mitochondrial ROS formation and respiratory dysfunction. This concept was supported by observations that ethidium bromide-induced mitochondrial d…

Mitochondrial ROSAgingPotassium ChannelsMyocytes Smooth MuscleBiophysicsIn Vitro TechniquesMitochondrionmedicine.disease_causeMitochondrial Membrane Transport ProteinsModels BiologicalMitochondrial apoptosis-induced channelBiochemistryPeroxynitritechemistry.chemical_compoundmedicineAnimalsHumansMitochondrionFeedback PhysiologicalNADPH oxidasebiologyNADPH oxidaseMitochondrial Permeability Transition PoreSuperoxideAngiotensin IINADPH OxidasesSuperoxideNitric oxideCell BiologyReactive Nitrogen SpeciesMitochondriaCell biologyOxidative StressOxidative protein modificationchemistryMitochondrial permeability transition poreRedox regulationNOX1Hypertensionbiology.proteinReactive Oxygen SpeciesOxidation-ReductionOxidative stressSignal TransductionBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Oxidant antioxidants and adaptive responses to exercise.

2015

The extensive damage produced by unaccustomed (acute) exercise and the health benefits of regular physical activity are well-known phenomena as well as the role played in them by reactive oxygen species (ROS). The present issue reports some interesting studies showing that the Janus faced effects of exercise-induced ROS in skeletal muscle. Most studies dealing with ROS contribution to acute exercise-induced tissue damage determine the levels of markers of oxidative damage to specific substances but they do not take into account total redox status of an individual before and after exercise. In their research article D. Stagos et al. used markers measuring plasma static (sORP) and capacity (c…

Mitochondrial ROSAgingmedicine.medical_specialtyArticle SubjectPhysical exerciseOxidative phosphorylationBiologymedicine.disease_causeBiochemistryAntioxidantsLipid peroxidationchemistry.chemical_compoundInternal medicinemedicineHumanslcsh:QH573-671Exercisechemistry.chemical_classificationReactive oxygen specieslcsh:CytologyCell BiologyGeneral MedicineOxidantsGlutathioneMitochondrial respiratory chainEndocrinologyEditorialchemistryBiochemistryExercise intensityReactive Oxygen SpeciesOxidative stressOxidative medicine and cellular longevity
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Reactive oxygen species derived from the mitochondrial respiratory chain are not responsible for the basal levels of oxidative base modifications obs…

2004

The mitochondrial electron transport chain (ETC) is the most important source of reactive oxygen species (ROS) in mammalian cells. To assess its relevance to the endogenous generation of oxidative DNA damage in the nucleus, we have compared the background (steady-state) levels of oxidative DNA base modifications sensitive to the repair glycosylase Fpg (mostly 7,8-dihydro-8-oxoguanine) in wild-type HeLa cells and HeLa rho0 cells. The latter are depleted of mitochondrial DNA and therefore are unable to produce ROS in the ETC. Although the levels of ROS measured by flow cytometry and redox-sensitive probes in rho0 cells were only 10-15% those of wild-type cells, steady-state levels of oxidativ…

Mitochondrial ROSCarbonyl Cyanide m-Chlorophenyl HydrazoneMitochondrial DNADNA damageCells[SDV]Life Sciences [q-bio]Oxidative phosphorylationMitochondrionBiologyBiochemistryElectron Transport03 medical and health sciences0302 clinical medicinePhysiology (medical)AnimalsHumansComputingMilieux_MISCELLANEOUS030304 developmental biologyCell Nucleus0303 health sciencesGuanosineNucleotidesEscherichia coli ProteinsDNAFlow CytometryMitochondriaNuclear DNAMitochondrial respiratory chainDNA-Formamidopyrimidine GlycosylaseBiochemistryDNA glycosylaseMacrolidesReactive Oxygen SpeciesOxidation-Reduction030217 neurology & neurosurgeryDNA DamageHeLa Cells
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Effects of a high-fat diet on energy metabolism and ROS production in rat liver.

2011

International audience; BACKGROUND & AIMS: A high-fat diet affects liver metabolism, leading to steatosis, a complex disorder related to insulin resistance and mitochondrial alterations. Steatosis is still poorly understood since diverse effects have been reported, depending on the different experimental models used. METHODS: We hereby report the effects of an 8 week high-fat diet on liver energy metabolism in a rat model, investigated in both isolated mitochondria and hepatocytes. RESULTS: Liver mass was unchanged but lipid content and composition were markedly affected. State-3 mitochondrial oxidative phosphorylation was inhibited, contrasting with unaffected cytochrome content. Oxidative…

Mitochondrial ROSMaleTranscription GeneticMESH : Reactive Oxygen SpeciesMitochondria LiverMESH : HepatocytesMitochondrionOxidative PhosphorylationMESH: Hepatocytes0302 clinical medicineMESH: Membrane Potential MitochondrialCitrate synthaseMESH: AnimalsBeta oxidationMESH : Electron Transport2. Zero hungerMembrane Potential Mitochondrial0303 health sciencesMESH : RatsAdenine nucleotide translocatorMESH: Energy MetabolismMESH: Reactive Oxygen SpeciesLipidsBiochemistryLiverMESH: Dietary FatsMitochondrial matrix030220 oncology & carcinogenesisBody CompositionMESH : Oxidative PhosphorylationATP–ADP translocaseMESH: Mitochondria LiverMESH: RatsMESH : Body CompositionMESH : MaleOxidative phosphorylationBiologyMESH : Rats WistarElectron Transport03 medical and health sciencesMESH: Oxidative Phosphorylation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRats WistarMESH: Electron Transport[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyHepatologyMESH: Transcription GeneticMESH : Transcription GeneticMESH : LiverMESH : LipidsMESH: Body CompositionMESH: Rats WistarMESH: LipidsDietary FatsMESH: MaleRatsMESH : Energy MetabolismMESH : Membrane Potential MitochondrialMESH : Mitochondria Liverbiology.proteinHepatocytesMESH : AnimalsEnergy MetabolismReactive Oxygen SpeciesMESH : Dietary FatsMESH: Liver
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Astrocytes Protect Neurons from Aβ1-42 Peptide-Induced Neurotoxicity Increasing TFAM and PGC-1 and Decreasing PPAR-γ and SIRT-1

2015

One of the earliest neuropathological events in Alzheimer's disease is accumulation of astrocytes at sites of Aβ1-42 depositions. Our results indicate that Aβ1-42 toxic peptide increases lipid peroxidation, apoptosis and cell death in neurons but not in astrocytes in primary culture. Aβ1-42-induced deleterious neuronal effects are not present when neurons and astrocytes are mixed cultured. Stimulation of astrocytes with toxic Aβ1-42 peptide increased p-65 and decreased IκB resulting in inflammatory process. In astrocytes Aβ1-42 decreases protein expressions of sirtuin 1 (SIRT-1) and peroxisome proliferator-activated receptor γ (PPAR-γ) and over-expresses peroxisome proliferator-activated re…

MnSODProgrammed cell deathPPAR-γPeroxisome proliferator-activated receptorMitochondrionBiologyBioinformaticsmedicine.disease_causeAlzheimer's DiseaseNeurologiaPGC-1Sirtuin 1medicineAnimalsTFAMCells Culturedchemistry.chemical_classificationNeuronsAmyloid beta-PeptidesCell DeathSirtuin 1Caspase 3Superoxide DismutaseNeurotoxicityTranscription Factor RelAGeneral MedicineTFAMmedicine.diseasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCoculture TechniquesPeptide FragmentsCell biologyMitochondriaPeroxidesRatsPPAR gammachemistryMitochondrial biogenesisNF-κB.Astrocytesbiology.proteinFisiologia humanaLipid PeroxidationOxidative stressResearch PaperTranscription FactorsInternational Journal of Medical Sciences
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In Silico Insights into the SARS CoV-2 Main Protease Suggest NADH Endogenous Defences in the Control of the Pandemic Coronavirus Infection

2020

COVID-19 is a pandemic health emergency faced by the entire world. The clinical treatment of the severe acute respiratory syndrome (SARS) CoV-2 is currently based on the experimental administration of HIV antiviral drugs, such as lopinavir, ritonavir, and remdesivir (a nucleotide analogue used for Ebola infection). This work proposes a repurposing process using a database containing approximately 8000 known drugs in synergy structure- and ligand-based studies by means of the molecular docking and descriptor-based protocol. The proposed in silico findings identified new potential SARS CoV-2 main protease (MPRO) inhibitors that fit in the catalytic binding site of SARS CoV-2 MPRO. Several sel…

Models Molecular0301 basic medicineAgingmedicine.medical_treatmentcoronaviruslcsh:QR1-502Viral Nonstructural Proteinsmedicine.disease_causelcsh:Microbiology0302 clinical medicineSettore BIO/10 - BiochimicaCoronavirus 3C ProteasesCoronavirusvirus diseasesLopinavirHypothesisMolecular Docking SimulationCysteine EndopeptidasesDrug repositioningInfectious Diseases030220 oncology & carcinogenesisCoronavirus InfectionsOxidation-Reductionmedicine.drugDNA damageIn silicoPneumonia ViralBiologyAntiviral AgentsHIV-proteaseBetacoronavirus03 medical and health sciencesSARS-CoV-2 main proteaseVirologymedicineHumansComputer SimulationProtease InhibitorsPandemicsBinding SitesProteaseSARS-CoV-2Drug RepositioningCOVID-19HIV Protease InhibitorsDRUDIT web servicemolecular dockingNADbiology.organism_classificationVirologySettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug Treatmentcoronaviru030104 developmental biologyNADHRitonavirBetacoronavirusDNA Damage
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Inhibitory effects and oxidation of 6-methylcoumarin, 7-methylcoumarin and 7-formylcoumarin via human CYP2A6 and its mouse and pig orthologous enzymes

2015

1. Information about the metabolism of compounds is essential in drug discovery and development, risk assessment of chemicals and further development of predictive methods. 2. In vitro and in silico methods were applied to evaluate the metabolic and inhibitory properties of 6-methylcoumarin, 7-methylcoumarin and 7-formylcoumarin with human CYP2A6, mouse CYP2A5 and pig CYP2A19. 3. 6-Methylcoumarin was oxidized to fluorescent 7-hydroxy-6-methylcoumarin by CYP2A6 (Km: 0.64-0.91 µM; Vmax: 0.81-0.89 min(-1)) and by CYP2A5 and CYP2A19. The reaction was almost completely inhibited at 10 µM 7-methylcoumarin in liver microsomes of human and mouse, but in pig only 40% inhibition was obtained with the…

Models Molecular0301 basic medicineenzyme assayTime Factorscoumarin derivativecytochrome P450Health Toxicology and MutagenesisIn silicoSus scrofaHydroxylationToxicologyta3111BiochemistryCytochrome P-450 CYP2A6Inhibitory Concentration 50Mice03 medical and health sciencesCoumarinsmedicineAnimalsCytochrome P-450 Enzyme InhibitorsHumansCYP2A6ta317Pharmacologychemistry.chemical_classificationbiologyMethoxsalenta1182Cytochrome P450General MedicineMetabolismMolecular biologyIn vitroEnzyme assayKinetics030104 developmental biologyEnzymeBiochemistrychemistrybiology.proteinfluorescenceOxidation-Reductionmetabolismmedicine.drugXenobiotica
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Cu(II) complexes with a sulfonamide derived from benzoguanamine. Oxidative cleavage of DNA in the presence of H2O2 and ascorbate

2004

Reaction between benzoguanamine (2,4-diamino-6-phenyl-1,3,5-triazine) and 2-mesitylenesulfonyl chloride leads to formation of a sulfonamide able to form two mononuclear Cu(II) complexes with a CuL(2) stoichiometry. The local environment of the metal cation is a distorted octahedron, with two ligands and two solvent molecules; both complexes crystallize in the monoclinic structure, space group P2(1), with Z=2. In the presence of ascorbate/H(2)O(2,) the two complexes significantly cleavage double-strand pUC18 DNA plasmid. Both complexes exhibit more nuclease efficiency that the copper phenantroline complex. From scavenging reactive oxygen studies we conclude that the hydroxyl radical and a si…

Models MolecularDNA damagechemistry.chemical_elementAscorbic AcidCrystallography X-RayCleavage (embryo)PhotochemistryGuanidinesBiochemistryPeroxideMedicinal chemistryInorganic ChemistryMetalchemistry.chemical_compoundOrganometallic CompoundsMoleculechemistry.chemical_classificationSulfonamidesMolecular StructureTriazinesDNAHydrogen PeroxideCopperSulfonamidechemistryvisual_artvisual_art.visual_art_mediumHydroxyl radicalOxidation-ReductionCopperJournal of Inorganic Biochemistry
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