Search results for "Redox"

showing 10 items of 619 documents

Oxidative stress responses and lipid peroxidation damage are induced during dehydration in the production of dry active wine yeasts.

2009

The tolerance of the yeast Saccharomyces cerevisiae to desiccation is important for the use of this microorganism in the wine industry, since active dry wine yeast is routinely used as starter for must fermentations. Many studies have shown the complexity of the cellular effects caused by water loss, including oxidative injuries on macromolecular components. However the technological interest of yeast drying was not addressed in those studies, and the dehydration conditions were far from the industrial practice. In the present study a molecular approach was used to characterize the relevant injuring conditions during pilot plant dehydrations under two different drying temperatures (i.e., 35…

Time FactorsWineSaccharomyces cerevisiaeBiologymedicine.disease_causeMicrobiologyLipid peroxidationchemistry.chemical_compoundIndustrial MicrobiologyGlutaredoxinGene Expression Regulation FungalmedicineBiomassDesiccationWinemakingWinefood and beveragesGeneral MedicineGlutathioneYeastYeast in winemakingOxidative StressBiochemistrychemistryFermentationLipid PeroxidationOxidation-ReductionOxidative stressFood ScienceInternational journal of food microbiology
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The Formal Redox Potential of the Ti(IV, III) Couple at 25 °C in 1 M HCl 2 M NaCl Medium

2007

The formal redox potential of the Ti(IV, III) couple has been determined at 25 degrees C in 1 M HCl, 2 M NaCl aqueous medium, by emf measurements of a junction-free cell with glass and mercury electrodes. Ti(III) and Ti(IV) concentrations were changed by controlled electrolysis. The mean value of the searched formal potential, in a large range of total titanium concentration, is 9 +/- 1 mV against the molar hydrogen electrode in the same ionic medium.

TitaniumElectrolysisStandard hydrogen electrodeInorganic chemistryTemperaturechemistry.chemical_elementIonic bondingSodium ChlorideTitanium redox equilibria Formal redox potentials Junction-free cells Electrolysis Constant ionic mediumEMF measurementElectrochemistryRedoxAnalytical Chemistrylaw.inventionchemistrylawElectrodeElectrochemistryHydrochloric AcidOxidation-ReductionGeneral Environmental ScienceTitaniumAnnali di Chimica
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A redox-sensitive nanofluidic diode based on nicotinamide-modified asymmetric nanopores

2017

[EN] We demonstrate a redox-sensitive nanofluidic diode whose ion rectification is modulated by the oxidation and reduction of chemical moieties incorporated on its surface. To achieve this goal, we have first synthesized the chemical compounds 1-(4-aminobutyl)-3-carbamoylpyridin-1-ium (Nic-BuNH2) and 3-carbamoyl-1-(2,4-dinitrophenyl)pyridinium (Nic-DNP). Then, the surface of track-etched single asymmetric nanopores is decorated with the redox-sensitive Nic-BuNH2 and Nic-DNP molecules using carbodiimide coupling chemistry and Zincke reaction, respectively. The success of the modification reactions is monitored through the changes in the current¿voltage (I¿V) curves prior to and after pore f…

Track-etchingReducing agent02 engineering and technology010402 general chemistryPhotochemistry01 natural sciencesRedoxIonchemistry.chemical_compoundMaterials ChemistryMoleculeOrganic chemistryRedox reactionSurface chargeElectrical and Electronic EngineeringNicotinamideInstrumentationCurrent rectificationMetals and Alloys021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsNanoporechemistrySurface functionalizationFISICA APLICADASurface modificationPyridiniumSynthetic nanopores0210 nano-technologySensors and Actuators B: Chemical
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Regulation of stress response in Oenococcus oeni as a function of environmental changes and growth phase

2000

International audience; Oenococcus oeni is a lactic acid bacterium which is able to grow in wine and perform malolactic fermentation. To survive and grow in such a harsh environment as wine, O. oeni uses several mechanisms of resistance including stress protein synthesis. The molecular characterisation of three stress genes hsp18, clpX, trxA encoding for a small heat shock protein, an ATPase regulation component of ClpP protease and a thioredoxin, respectively, allow us to suggest the existence in O. oeni of multiple regulation mechanisms as is the case in Bacillus subtilis. One common feature of these genes is that they are expressed under the control of housekeeping promoters. The express…

Transcription Geneticmedicine.medical_treatment[SDV]Life Sciences [q-bio]bactérie lactiqueBacillus subtilisatpaseMicrobiologygène clppoenococcus oenicaractérisation moléculaire03 medical and health sciencesBacterial ProteinsHeat shock proteinOenococcus;Malolactic fermentation;Stress gene;ATPaseMalolactic fermentationmedicineprotéine de choc thermiquePromoter Regions GeneticGeneHeat-Shock ProteinsOenococcus030304 developmental biologyOenococcus oeniAdenosine Triphosphatases0303 health sciencesProteasebiology030306 microbiologyMalolactic fermentationStress genefood and beveragesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationGram-Positive CocciBiochemistryThioredoxinOenococcusLeuconostocFood Scienceexpression des gènes
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Trinuclear Mo3S7 clusters coordinated to dithiolate or diselenolate ligands and their use in the preparation of magnetic single component molecular c…

2008

A general route for the preparation of a series of dianionic Mo3S7 cluster complexes bearing dithiolate or diselenolate ligands, namely, [Mo3S7L3](2-) (where L = tfd (bis(trifluoromethyl)-1,2-dithiolate) (4(2-)), bdt (1,2-benzenedithiolate) (5(2-)), dmid (1,3-dithia-2-one-4,5-dithiolate) (6(2-)), and dsit (1,3-dithia-2-thione-4,5-diselenolate) (7(2-))) is reported by direct reaction of [Mo3S7Br6](2-) and (n-Bu)2Sn(dithiolate). The redox properties, molecular structure, and electronic structure (BP86/VTZP) of the 4(2-) to 7(2-) clusters have also been investigated. The HOMO orbital in all complexes is delocalized over the ligand and the Mo3S7 cluster core. Ligand contributions to the HOMO ra…

Trifluoromethyl010405 organic chemistryStereochemistryLigand[CHIM.ORGA]Chemical Sciences/Organic chemistryElectronic structure010402 general chemistry01 natural sciencesRedox0104 chemical sciencesInorganic Chemistrychemistry.chemical_compoundCrystallographyDelocalized electronAtomic orbitalchemistryCluster (physics)MoleculePhysical and Theoretical ChemistryComputingMilieux_MISCELLANEOUSInorganic chemistry
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Methylation as an effective way to generate SOD-activity in copper complexes of scorpiand-like azamacrocyclic receptors

2018

Abstract Methylation of the secondary amine groups of a scorpiand-type ligand consisting of a pyridine spacer connected through methylene groups to a tris(2-aminomethyl) unit with the pendant arm further functionalised with a 3-pyridine unit leads to a ligand whose Cu(II) complex exhibits threefold enhanced SOD activity with respect to the non-methylated ligand. Potentiometric studies indicate the formation of [CuL] 2+ species with a stability three orders of magnitude lower than that formed with the related non-methylated ligand. Kinetic studies indicate that methylation of the secondary nitrogens causes a deceleration of both the complex formation and the acid-induced dissociation of the …

Tris010405 organic chemistryChemistryPotentiometric titration010402 general chemistryPhotochemistry01 natural sciencesMedicinal chemistryRedoxDissociation (chemistry)0104 chemical sciencesInorganic ChemistryMetalchemistry.chemical_compoundvisual_artPyridineMaterials Chemistryvisual_art.visual_art_mediumAmine gas treatingPhysical and Theoretical ChemistryMethyleneInorganica Chimica Acta
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Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase–Inhibitor Complex

2020

Abstract The absence of fluorine from most biomolecules renders it an excellent probe for NMR spectroscopy to monitor inhibitor–protein interactions. However, predicting the binding mode of a fluorinated ligand from a chemical shift (or vice versa) has been challenging due to the high electron density of the fluorine atom. Nonetheless, reliable 19F chemical‐shift predictions to deduce ligand‐binding modes hold great potential for in silico drug design. Herein, we present a systematic QM/MM study to predict the 19F NMR chemical shifts of a covalently bound fluorinated inhibitor to the essential oxidoreductase tryparedoxin (Tpx) from African trypanosomes, the causative agent of African sleepi…

Trypanosoma brucei bruceiProtozoan ProteinsContext (language use)PyrimidinonesThiophenes010402 general chemistry01 natural sciencesCatalysisquantum chemistryThioredoxinsNMR spectroscopyComputational chemistryOxidoreductasestructural biologyEnzyme InhibitorsNuclear Magnetic Resonance Biomolecularchemistry.chemical_classificationAfrican sleeping sickness010405 organic chemistryChemistryChemical shiftCommunicationGeneral ChemistryNuclear magnetic resonance spectroscopyFluorineOxidoreductase inhibitorLigand (biochemistry)Trypanocidal AgentsCommunications0104 chemical sciencesStructural biologyCovalent bondddc:540Mutationcovalent inhibitorsProtein BindingAngewandte Chemie (International Ed. in English)
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Inhibitor-Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes

2018

Trypanosomal and leishmanial infections claim tens of thousands of lives each year. The metabolism of these unicellular eukaryotic parasites differs from the human host and their enzymes thus constitute promising drug targets. Tryparedoxin (Tpx) from Trypanosoma brucei is the essential oxidoreductase in the parasite's hydroperoxide-clearance cascade. In vitro and in vivo functional assays show that a small, selective inhibitor efficiently inhibits Tpx. With X-ray crystallography, SAXS, analytical SEC, SEC-MALS, MD simulations, ITC, and NMR spectroscopy, we show how covalent binding of this monofunctional inhibitor leads to Tpx dimerization. Intra- and intermolecular inhibitor-inhibitor, pro…

TrypanosomaProtein ConformationSpermidineDimerTrypanosoma brucei bruceiAntiprotozoal AgentsMolecular Dynamics SimulationTrypanosoma brucei010402 general chemistry01 natural sciencesCatalysischemistry.chemical_compoundThioredoxinsBacterial ProteinsIn vivoOxidoreductaseAnimalsHumansEnzyme Inhibitorschemistry.chemical_classificationbiology010405 organic chemistryHydrogen PeroxideGeneral ChemistryNuclear magnetic resonance spectroscopyLigand (biochemistry)biology.organism_classificationGlutathione0104 chemical sciencesEnzymechemistryBiochemistryDrug DesignChemically induced dimerizationProtein MultimerizationOxidoreductasesOxidation-ReductionProtein BindingAngewandte Chemie International Edition
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Oxidation of carbidopa by tyrosinase and its effect on murine melanoma

2009

Oxidation of the anti-Parkinsonian agent carbidopa by tyrosinase was investigated. The products of this reaction were identified as 3-(3,4-dihydroxyphenyl)-2-methylpropanoic acid and 6,7-dihydroxy-3-methylcinnoline. These results demonstrate that after oxidation of the catechol moiety to an o-quinone either a redox exchange with the hydrazine group or a cyclization reaction occur. The cyclization product underwent additional oxidation reactions leading to aromatization. The cyclization reaction is undesired in the case of hydrazine-containing anti-melanoma prodrugs and will have to be taken into account in designing such compounds. Carbidopa was tested against B16(F10) melanoma cells in cul…

TyrosinaseClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentstyrosinaseBiochemistryRedoxMicechemistry.chemical_compoundCell Line TumorDrug DiscoverymedicinemelanomaAnimalsMoietyOrganic chemistryProdrugscarbidopaCytotoxicityMolecular BiologyCatecholMonophenol MonooxygenaseChemistryOrganic ChemistryAromatizationhydrazineProdrugCombinatorial chemistryDihydroxyphenylalanineCyclizationCarbidopaMolecular MedicineprodrugOxidation-Reductionmedicine.drugBioorganic & Medicinal Chemistry Letters : a tetrahedron publication for the rapid dissemination of preliminary communication and all aspects of bioorganic chemistry, medicinal chemistry and related disciplines
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Indirect oxidation of the antitumor agent procarbazine by tyrosinase—Possible application in designing anti-melanoma prodrugs

2008

The interaction of tyrosinase with the anticancer drug procarbazine has been investigated. In the presence of the enzyme alone no oxidation of this dialkylhydrazine above the background level was observed. However, when phenolic substrates (4-tert-butylcatechol or N-acetyl-l-tyrosine) were included in the reaction mixture, procarbazine was rapidly degraded. Oxygen consumption measurements showed that in a mixture both the phenolic substrate and the drug were oxidized. The major product of procarbazine degradation was isolated and identified as azoprocarbazine, the first active metabolite of this drug detected in previous in vivo and in vitro studies. This indirect oxidation of the hydrazine…

TyrosinaseClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentstyrosinaseProcarbazineBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundOxygen ConsumptionIn vivoDrug DiscoverymelanomamedicineOrganic chemistryProdrugsHydrazine (antidepressant)PhenolsMolecular BiologyActive metaboliteMolecular StructureMonophenol MonooxygenaseOrganic ChemistrySubstrate (chemistry)hydrazineProdrugHydrazineschemistryProcarbazineMolecular Medicineredox exchangeprodrugAgaricalesOxidation-Reductionmedicine.drugBioorganic & Medicinal Chemistry Letters
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