Search results for "Oxidation-Reduction"

showing 10 items of 689 documents

Direct measurement of the melting temperature of supported DNA by electrochemical method

2003

The development of biosensors based on DNA hybridization requires a more precise knowledge of the thermodynamics of the hybridization at a solid interface. In particular, the selectivity of hybridization can be affected by a lot of parameters such as the single-strand (ss)DNA density, the pH, the ionic strength or the temperature. The melting temperature, T(m), is in part a function of the ionic strength and of the temperature and therefore provides a useful variable in the control of the selectivity and sensitivity of a DNA chip. The electrochemical technique has been used to determine the T(m) values when the probe is tethered by a DNA self-assembled monolayer (SAM). We have built a speci…

Osmolar ConcentrationTemperatureAnalytical chemistryDNABiologyNucleic Acid DenaturationElectrochemistrySensitivity and SpecificityMolecular biologyRedox indicatorIonic strengthMonolayerElectrodeElectrochemistryGeneticsThermodynamicsA-DNASelectivityElectrodesOxidation-ReductionBiosensorNAR Methods OnlineOligonucleotide Array Sequence AnalysisNucleic Acids Research
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Molecular and electronic structure of square-planar nickel(ii), nickel(iii) and nickel(iii)π-cation radical complexes with a tetradentate o-phenylene…

2005

The molecular and electronic structures of the electron transfer series of four-coordinate square-planar nickel complexes with the ligand o-phenylenebis(N'-methyloxamidate), [NiL]z (z = 2-, 1-, 0), have been evaluated by DFT and TDDFT calculations, and most of their experimentally available structural and spectroscopic properties (X. Ottenwaelder et al., Dalton Trans., 2005, DOI: 10.1039/b502478a) have been reasonably reproduced at the B3LYP level of theory. The anionic species [NiL]2- and [NiL]- are genuine low-spin nickel II and nickel III complexes with diamagnetic singlet (S = 0) and paramagnetic doublet (S = 1/2) states, respectively. The nickel III complex presents shorter Ni-N(amidat…

OxalatesFree RadicalsMolecular StructureLigandchemistry.chemical_elementElectronsPhenylenediaminesLigandsPhotochemistryInorganic ChemistryParamagnetismElectron transferCrystallographyNickelModels ChemicalchemistryNickelCovalent bondCationsExcited stateOrganometallic CompoundsQuantum TheorySinglet stateGround stateOxidation-ReductionDalton Transactions
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Flow-chemiluminescence: a growing modality of pharmaceutical analysis.

2001

The present article deals with a review of the applications of the chemiluminescence to pharmaceutical analyses by using continuous-flow assemblies. A comprehensive study on the fundamentals of the chemiluminescence is also included.

OxalatesMaterials scienceModality (human–computer interaction)LuminescenceLuminescent MeasurementsMolecular StructureContinuous flowChemistry PharmaceuticalBiophysicsImidazolesOxidation reductionlaw.invention22'-DipyridylChemical engineeringFlow (mathematics)Chemistry (miscellaneous)lawCoordination ComplexesLuminescent MeasurementsAnimalsIndicators and ReagentsLuminolOxidation-ReductionChemiluminescenceFluorescent DyesLuminescence : the journal of biological and chemical luminescence
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Pro-oxidant effects of 7-hydroperoxycholest-5-en-3β-ol on the copper-initiated oxidation of low density lipoprotein

1995

AbstractIn low density lipoproteins (LDL) supplemented with aged cholesterol and oxidized in the presence of Cu2+, an increase of the lipid oxidation parameters was observed compared with pure cholesterol-enriched LDL. A compound, identified as 7-hydroperoxycholesterol (7HPC), isolated from aged cholesterol and added to LDL, reproduced the above effects. The results indicate that the pro-oxidant effect of 7HPC is dependent on the hydroperoxy group since the corresponding alcohol derivative, 7α-hydroxycholesterol, had no such effect. These data suggest that among the LDL-associated lipid peroxides, cholesterol peroxides may have important implications in the susceptibility of this lipoprotei…

Oxidized LDLLipid PeroxidesVery low-density lipoproteinTime FactorsOxysterolBiophysicsBiochemistryMedicinal chemistrychemistry.chemical_compoundOxysterolLipid oxidationStructural BiologyOxidationGeneticsHumansMolecular BiologyIntermediate-density lipoproteinCholesterolCell BiologyOxidantsPro-oxidantLipoproteins LDLCholesterolchemistryLow-density lipoproteinCholesterol hydroperoxidelipids (amino acids peptides and proteins)Oxidation-ReductionAged cholesterolCopperLipoproteinFEBS Letters
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C172S Substitution in the Chloroplast-encoded Large Subunit Affects Stability and Stress-induced Turnover of Ribulose-1,5-bisphosphate Carboxylase/Ox…

1999

Previous work has indicated that the turnover of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1. 39) may be controlled by the redox state of certain cysteine residues. To test this hypothesis, directed mutagenesis and chloroplast transformation were employed to create a C172S substitution in the Rubisco large subunit of the green alga Chlamydomonas reinhardtii. The C172S mutant strain was not substantially different from the wild type with respect to growth rate, and the purified mutant enzyme had a normal circular dichroism spectrum. However, the mutant enzyme was inactivated faster than the wild-type enzyme at 40 and 50 degrees C. In contrast, C172S mutant …

OxygenaseChloroplastsProtein ConformationRibulose-Bisphosphate CarboxylaseMutantChlamydomonas reinhardtiiBiochemistrychemistry.chemical_compoundEnzyme StabilitySerineAnimalsCysteineMolecular BiologyCysteine metabolismRibulose 15-bisphosphatebiologyCircular DichroismRuBisCOWild typeCell Biologybiology.organism_classificationChloroplastPhenotypeAmino Acid SubstitutionchemistryBiochemistryMutagenesis Site-Directedbiology.proteinSpectrophotometry UltravioletOxidation-ReductionChlamydomonas reinhardtiiJournal of Biological Chemistry
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Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocatio…

2006

The role of cysteines 449 (Cys449) and 459 (Cys459) from the large subunit (LS) of ribulose 1-5-bisphosphate carboxylase/oxygenase (Rubisco) in the reduction-oxidation (redox) regulation of the enzyme was assessed by site-directed mutagenesis of these residues and chloroplast transformation of Chlamydomonas reinhardtii. In vitro studies indicated that mutations C449S, C459S or C449S/ C459S do not affect the activity and proteolytic susceptibility of the enzyme in the reduced state. However, when oxidized, the mutant enzymes differed from the wild type (WT), showing an increased resistance to inactivation and, in the case of the double mutant (DM), an altered structural conformation as refle…

OxygenaseProtein ConformationPhysiologyRibulose-Bisphosphate CarboxylaseBlotting WesternChlamydomonas reinhardtiiPlant ScienceBiologychemistry.chemical_compoundCysteinechemistry.chemical_classificationRibulose 15-bisphosphateRibuloseCell MembraneRuBisCOWild typebiology.organism_classificationPyruvate carboxylaseProtein TransportEnzymeBiochemistrychemistryMutagenesis Site-Directedbiology.proteinElectrophoresis Polyacrylamide GelOxidation-ReductionPlant, Cell and Environment
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Modification of the proteolytic fragmentation pattern upon oxidation of cysteines from ribulose 1,5-bisphosphate carboxylase/oxygenase.

2003

The proteolytic susceptibility of the native CO 2 -fixing photosynthetic enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39, Rubisco) has been shown to increase in vitro after oxidative treatments that affect cysteine thiols. A limited incubation of oxidized (pretreated with the disulfide cystamine) Rubisco from Chlamydomonas reinhardtii with subtilisin or proteinase K generated fragments of molecular mass about 53 kDa (band I in SDS-PAGE) and 47 kDa (band II) derived from the large subunit (55 kDa) of the enzyme. In contrast, proteolysis of the reduced Rubisco (pretreated with the free thiol cysteamine) produced only the 53 kDa band. The same fragmentation pattern was repr…

OxygenaseProtein subunitRibulose-Bisphosphate CarboxylaseMolecular Sequence DataBiochemistrychemistry.chemical_compoundEndopeptidasesAnimalsEuglena gracilisAmino Acid SequenceCysteineConserved SequenceRibulose 15-bisphosphatebiologyRibuloseHydrolysisfungiRuBisCOSubtilisinPeptide FragmentsKineticsProtein SubunitschemistryBiochemistryModels Chemicalbiology.proteinProtein quaternary structureHoloenzymesOxidation-ReductionProtein Processing Post-TranslationalChlamydomonas reinhardtiiCysteineBiochemistry
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Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments

1990

The susceptibility of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolysis by trypsin, chymotrypsin, proteinase K, and papain is enhanced by oxidative treatments including spontaneous oxidation of cysteines. Proteinases exhibit a high specificity for the oxidized inactive form of the carboxylase, cleaving its large subunit. Treatment of the inactive enzyme with dithiothreitol results in partial recovery of both carboxylase activity and resistance to proteolysis. This behavior may explain the specific degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase that occurs in vivo during leaf senescence.

OxygenaseTime FactorsRibulose-Bisphosphate CarboxylaseProteolysisBiophysicsBiochemistryDithiothreitolchemistry.chemical_compoundEnzyme StabilitymedicineCysteineMolecular Biologychemistry.chemical_classificationChymotrypsinRibulose 15-bisphosphatebiologymedicine.diagnostic_testHydrolysisPlantsTrypsinPyruvate carboxylaseEnzymechemistryBiochemistrybiology.proteinOxidation-ReductionPeptide Hydrolasesmedicine.drugArchives of Biochemistry and Biophysics
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Influence of the functionalisation of mesoporous silica material UVM-7 on polyphenol oxidase enzyme capture and enzymatic browning

2020

Polyphenol oxidase (PPO), also known as tyrosinase and catechol oxidase, is the enzyme responsible for enzymatic browning in foods. It causes undesirable organoleptic, nutritional and colour changes. Here, we report the preparation of five nanomaterials and a study of their ability to modulate PPO enzyme activity. The materials consist of UVM-7 supports (a mesoporous silica material) modified with diverse functional groups (i.e. amine, carboxylic acid, isocyanate, alkane and pyridine). We also studied the PPO immobilisation capability of the materials. All the materials, except the carboxylic acid functionalised one, offer high PPO loading capabilities and the immobilisation speed increases…

PPOTECNOLOGIA DE ALIMENTOSPyridinesSurface PropertiesApple juiceCarboxylic acidTyrosinaseCarboxylic AcidsUVM-701 natural sciencesPolyphenol oxidaseAnalytical Chemistry0404 agricultural biotechnologyQUIMICA ORGANICABrowningOrganic chemistryAminesCatechol oxidaseEdetic AcidInhibitionchemistry.chemical_classificationbiology010401 analytical chemistryQUIMICA INORGANICA04 agricultural and veterinary sciencesGeneral MedicineMesoporous silicaEnzymes ImmobilizedSilicon Dioxide040401 food scienceEnzyme assay0104 chemical sciencesNanostructuresFruit and Vegetable JuicesOxygenchemistryMalusbiology.proteinAmine gas treatingTyrosinaseOxidation-ReductionCatechol OxidaseFood Science
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Multi-Functional Nanogels for Tumor Targeting and Redox-Sensitive Drug and siRNA Delivery

2016

(1) Background: A new family of nanosystems able to discern between normal and tumor cells and to release a therapeutic agent in controlled way were synthetized by e-beam irradiation. This technique permits to obtain biocompatible, sterile, carboxyl-functionalized polyvinylpyrrolidone (PVP-co-acrylic acid) nanogels (NGs); (2) Methods: Here, we performed a targeting strategy based on the recognition of over-expressed proteins on tumor cells, like the folate receptor. The selective targeting was demonstrated by co-culture studies and flow cytometry analysis, using folate conjugated NGs. Moreover, nanoparticles were conjugated to a chemotherapeutic drug or to a pro-apoptotic siRNA through a gl…

PVPPharmaceutical ScienceNanogels02 engineering and technologyPharmacology01 natural sciencesAntioxidantsAnalytical Chemistryfolate-targetingPolyethylene GlycolsNanogelchemistry.chemical_compoundMiceRNA interferenceNeoplasmsDrug DiscoveryFluorescence microscopePolyethyleneimineRNA Small InterferingCytotoxicitymedicine.diagnostic_testPovidone021001 nanoscience & nanotechnologyControlled releaseCell biologyChemistry (miscellaneous)Folate receptorMolecular Medicinee-beamGSH-responsive release0210 nano-technologyOxidation-Reduction010402 general chemistrydoxorubicinArticleFlow cytometryFolic AcidCell Line TumormedicineAnimalsHumansPhysical and Theoretical ChemistryParticle SizeOrganic ChemistryGlutathione0104 chemical scienceschemistryPVP; nanogels; e-beam; folate-targeting; doxorubicin; siRNA; GSH-responsive releasesiRNACancer cellNIH 3T3 CellsNanoparticlesSettore CHIM/07 - Fondamenti Chimici Delle TecnologieFolic Acid TransportersHeLa CellsMolecules
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