Search results for "OXIDATION"

showing 10 items of 1913 documents

Biomarkers of lipid peroxidation in the aqueous humor of primary open-angle glaucoma patients

2016

Objective To investigate the lipid peroxidation (PEROX) processes in primary open-angle glaucoma (POAG) patients, and whether this mechanism may be related to disease progression. Material and methods A prospective, observational, cross-sectional, non-experimental, and analytical study was conducted on a case and a comparison group, consisting of 175 surgical patients divided into: (1) POAG group (GG; n = 88) and (2) comparison group of patients with cataracts (CG; n = 87). Demographic data, patient characteristics, lifestyle data, as well as ophthalmological examination were registered in an Excel spreadsheet. Biochemical data were obtained by processing the aqueous humor collected at the …

Intraocular pressuremedicine.medical_specialtygenetic structuresThiobarbituric acidGlaucomaGastroenterologyLipid peroxidation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineInternal medicineTBARSmedicineProspective cohort studySedentary lifestylebusiness.industryGeneral MedicineMalondialdehydemedicine.diseaseeye diseaseschemistryBiochemistry030221 ophthalmology & optometrysense organsbusiness030217 neurology & neurosurgeryArchivos de la Sociedad Española de Oftalmología (English Edition)
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IONIC LIQUIDS MODIFIED CATALYSTS: SYNTHESIS, IMMOBILIZATION AND USES.

Synthesis, catalytic activity and recovery of Ionic liquid modified and un-modified catalysts have mainly been focused in this thesis. Particularly, our attention has been given to 2,2,6,6-Tetramethyl-piperidine-N-oxyl (TEMPO) catalyst for its unique redox behavior in alcohol oxidation to carbonyl compounds. In order to tag appropriate number of IL moieties, [60]Fullerene as well as benzylic linker units were employed as a molecular support. However, covalently supported catalysts were recovered by a short silica pad while, ionic liquid-tagged TEMPO catalysts were recovered by a non-covalent “Release and Catch” approach using silica grafted polymeric multilayered covalently supported ionic …

Ionic Liquids TEMPO Oxidation Organo Catalysis Release and Catch.Settore CHIM/06 - Chimica Organica
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Dynamics of closure of zinc bis-porphyrin molecular tweezers with copper(II) ions and electron transfer.

2011

Zinc bis-porphyrin molecular tweezers composed of a N(4) spacer bound through pyridyl units to the meso position of porphyrins were synthesized, and the tweezers are closed by the coordination of a copper(II) ion inside the spacer ligand. The effect of the π-π interaction between the porphyrin rings in the closed conformation on the absorption spectra of multi-electron oxidized species and the reduction potentials were clarified by chemical and electrochemical oxidation of the closed form of the zinc bis-porphyrin molecular tweezers in comparison with the open form without copper(II) ion and the corresponding porphyrin monomer. The shifts in redox potentials and absorption spectrum of the p…

IonsLigandMetalloporphyrinsOrganic Chemistrychemistry.chemical_elementGeneral ChemistryZincElectrochemical TechniquesPhotochemistryPorphyrinCopperCatalysisDicationElectron TransportElectron transferchemistry.chemical_compoundchemistryTweezerspolycyclic compoundsheterocyclic compoundsSpectrophotometry UltravioletMolecular tweezersOxidation-ReductionCopperChemistry (Weinheim an der Bergstrasse, Germany)
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Iron, oxidative stress, and redox signaling in the cardiovascular system.

2014

The redox state of the cell is predominantly dependent on an iron redox couple and is maintained within strict physiological limits. Iron is an essential metal for hemoglobin synthesis in erythrocytes, for oxidation-reduction reactions, and for cellular proliferation. The maintenance of stable iron concentrations requires the coordinated regulation of iron transport into plasma from dietary sources in the duodenum, from recycled senescent red cells in macrophages, and from storage in hepatocytes. The absorption of dietary iron, which is present in heme or nonheme form, is carried out by mature villus enterocytes of the duodenum and proximal jejunum. Multiple physiological processes are invo…

Iron Overloadmedicine.disease_causeRedoxCardiovascular Systemchemistry.chemical_compound[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemHepcidinExtracellularmedicineAnimalsHumansHemeTranscription factorComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationReactive oxygen speciesbiologyOxidants[SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemOxidative StresschemistryBiochemistryCardiovascular Diseasesbiology.proteinOxidation-ReductionIntracellularOxidative stressIron DietaryFood ScienceBiotechnologySignal TransductionMolecular nutritionfood research
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Electrochemistry of Iron-Doped Zircon and Zirconia Materials and Electrocatalytic Effects on Nitrite Oxidation and Reduction

2014

Iron dopedRenewable Energy Sustainability and the EnvironmentChemistryInorganic chemistryCondensed Matter PhysicsElectrochemistrySurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsReduction (complexity)Nitrite oxidationMaterials ChemistryElectrochemistryCubic zirconiaZirconJournal of The Electrochemical Society
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Fast and direct analysis of oxidation levels of oil-in-water emulsions using ATR-FTIR.

2019

International audience; Oxidation of omega-3 fatty acids is a major limitation on its enrichment in food and beverages. An efficient and simple method to monitor lipid oxidation in complex systems is essential to limit lipid oxidation during formulation and processing. Fish oil-in-water emulsions (20% v/v) were exposed to iron or free radical initiated oxidation. Conjugated dienes (CDs) were rapidly measured using a previously developed fat extraction method. Fourier transform infrared (FTIR) spectroscopy has been used to directly record chemical changes occurring during oxidation. Variations were noticed in different spectral regions despite the presence of broad water bands near 3400 and …

IronAnalytical chemistryInfrared spectroscopyFish oil01 natural sciencesAnalytical ChemistryChemometrics0404 agricultural biotechnologyFish OilsLipid oxidation[SDV.IDA]Life Sciences [q-bio]/Food engineeringPartial least squares regressionFatty Acids Omega-3Spectroscopy Fourier Transform InfraredChemometricsFourier transform infrared spectroscopyLeast-Squares AnalysisSpectroscopyInfrared spectroscopyChemistryOil-in-water emulsions010401 analytical chemistryExtraction (chemistry)Water04 agricultural and veterinary sciencesGeneral Medicine[SDV.IDA] Life Sciences [q-bio]/Food engineering040401 food scienceLipid oxidation0104 chemical sciencesRadical initiatorRadical initiatorEmulsions[CHIM.OTHE]Chemical Sciences/OtherOxidation-ReductionFood ScienceFood chemistry
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Intramolecular electron transfer between molybdenum and iron mimicking bacterial sulphite dehydrogenase

2014

Diferrocenyl/diferrocenium substituted dioxido molybdenum(VI) complexes [Fe2MoO2] 2(Fc)/[2(FC)]²⁺ mimic the catalytic active site including the redox subunits as well as the catalytic function of bacterial sulphite oxidases.

IronSulfite DehydrogenaseMolecular Conformationchemistry.chemical_elementBiocompatible MaterialsElectronsCrystallography X-RayPhotochemistryRedoxCatalysisCatalysisElectron TransportElectron transferCoordination ComplexesCatalytic DomainPolymer chemistryMaterials ChemistrySulfite dehydrogenaseFerrous CompoundsMolybdenumBacteriabiologyMetals and AlloysActive siteGeneral ChemistryElectron transport chainSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryMolybdenumIntramolecular forceCeramics and Compositesbiology.proteinOxidation-ReductionChemical Communications
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Reduced Apo-Fumarate Nitrate Reductase Regulator (ApoFNR) as the Major Form of FNR in Aerobically Growing Escherichia coli▿

2008

ABSTRACT Under anoxic conditions, the Escherichia coli oxygen sensor FNR (fumarate nitrate reductase regulator) is in the active state and contains a [4Fe-4S] cluster. Oxygen converts [4Fe-4S]FNR to inactive [2Fe-2S]FNR. After prolonged exposure to air in vitro, apoFNR lacking a Fe-S cluster is formed. ApoFNR can be differentiated from Fe-S-containing forms by the accessibility of the five Cys thiol residues, four of which serve as ligands for the Fe-S cluster. The presence of apoFNR in aerobically and anaerobically grown E. coli was analyzed in situ using thiol reagents. In anaerobically and aerobically grown cells, the membrane-permeable monobromobimane labeled one to two and four Cys res…

Iron-Sulfur ProteinsAerobic bacteriamedicine.disease_causeNitrate reductaseMicrobiologymedicineEscherichia coliAnaerobiosisDisulfidesMolecular BiologyEscherichia colichemistry.chemical_classificationbiologySuccinate dehydrogenaseEscherichia coli Proteinsbiology.organism_classificationEnterobacteriaceaeEnzymes and ProteinsAerobiosisCulture MediaOxygenchemistryBiochemistryThiolbiology.proteinbacteriaAnaerobic bacteriaOxidation-ReductionBacteria
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O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli

1996

With an oxystat, changes in the pattern of expression of FNR-dependent genes from Escherichia coli were studied as a function of the O2 tension (pO2) in the medium. Expression of all four tested genes was decreased by increasing O2. However, the pO2 values that gave rise to half-maximal repression (pO(0.5)) were dependent on the particular promoter and varied between 1 and 5 millibars (1 bar = 10(5) Pa). The pO(0.5) value for the ArcA-regulated succinate dehydrogenase genes was in the same range (pO(0.5) = 4.6 millibars). At these pO2 values, the cytoplasm can be calculated to be well supplied with O2 by diffusion. Therefore, intracellular O2 could provide the signal to FNR, suggesting that…

Iron-Sulfur ProteinsCellular respirationRepressorBiologymedicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsGenes RegulatorEscherichia colimedicineAnaerobiosisMolecular BiologyEscherichia coliRegulation of gene expressionchemistry.chemical_classificationEscherichia coli ProteinsSuccinate dehydrogenaseMembrane ProteinsGene Expression Regulation BacterialElectron transport chainAerobiosisOxygenRepressor ProteinsSuccinate DehydrogenaseEnzymeLac OperonchemistryBiochemistryGenes BacterialMutationbiology.proteinOxidation-ReductionProtein KinasesIntracellularBacterial Outer Membrane ProteinsSignal TransductionResearch ArticleJournal of Bacteriology
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The oxidation of ubiquinol by the isolated rieske iron-sulfur protein in solution

1990

The pre-steady-state redox reactions of the Rieske iron-sulfur protein isolated from beef heart mitochondria have been characterized. The rates of oxidation by c-type cytochromes is much faster than the rate of reduction by ubiquinols. This enables the monitoring of the oxidation of ubiquinols by the Rieske protein through the steady-state electron transfer to cytochrome c in solution. The pH and ionic strength dependence of this reaction indicate that the ubiquinol anion is the direct reductant of the oxidized cluster of the iron-sulfur protein. The second electron from ubiquinol is diverted to oxygen by the isolated Rieske protein, and forms oxygen radicals that contribute to the steady-s…

Iron-Sulfur ProteinsUbiquinolCytochromeUbiquinoneBiophysicsmacromolecular substancesPhotochemistryBiochemistryRedoxMitochondria HeartElectron Transport Complex IIIElectron transferchemistry.chemical_compoundCytochrome C1AnimalsMolecular BiologybiologyChemistryCytochrome cHydrogen-Ion ConcentrationSolutionsKineticsCoenzyme Q – cytochrome c reductaseRieske proteinbiology.proteinCytochromesCattleOxidation-ReductionArchives of Biochemistry and Biophysics
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