Search results for "Kinetic"

showing 10 items of 3064 documents

De-epoxidation of Violaxanthin in Light-harvesting Complex I Proteins

2004

The conversion of violaxanthin (Vx) to zeaxanthin (Zx) in the de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of chloroplasts against photooxidative damage. Vx is bound to the antenna proteins of both photosystems. In photosystem II, the formation of Zx is essential for the pH-dependent dissipation of excess light energy as heat. The function of Zx in photosystem I is still unclear. In this work we investigated the de-epoxidation characteristics of light-harvesting complex proteins of photosystem I (LHCI) under in vivo and in vitro conditions. Recombinant LHCI (Lhcal-4) proteins were reconstituted with Vx and lutein, and the convertibility of Vx wa…

ChlorophyllLuteinPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesXanthophyllsPhotosystem IThylakoidsBiochemistrychemistry.chemical_compoundSolanum lycopersicumSpinacia oleraceaEscherichia coliMolecular BiologyPhotosystemchemistry.chemical_classificationBinding SitesPhotosystem I Protein ComplexChemistryfood and beveragesPigments BiologicalCell Biologybeta CaroteneRecombinant ProteinsChloroplastKineticsBiochemistryXanthophyllThylakoidEpoxy CompoundsApoproteinsViolaxanthinJournal of Biological Chemistry
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Early folding events during light harvesting complex II assembly in vitro monitored by pulsed electron paramagnetic resonance

2016

Efficient energy transfer in the major light harvesting complex II (LHCII) of green plants is facilitated by the precise alignment of pigments due to the protein matrix they are bound to. Much is known about the import of the LHCII apoprotein into the chloroplast via the TOC/TIC system and its targeting to the thylakoid membrane but information is sparse about when and where the pigments are bound and how this is coordinated with protein folding. In vitro, the LHCII apoprotein spontaneously folds and binds its pigments if the detergent-solubilized protein is combined with a mixture of chlorophylls a and b and carotenoids. In the present work, we employed this approach to study apoprotein fo…

ChlorophyllModels Molecular0301 basic medicineProtein FoldingPigment bindingLight-Harvesting Protein ComplexesBiophysicsBiochemistrylaw.invention03 medical and health scienceslawElectron paramagnetic resonancePlant ProteinsPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyProtein tertiary structureProtein Structure TertiaryChloroplastFolding (chemistry)KineticsCrystallography030104 developmental biologyEnergy TransferThylakoidProtein foldingApoproteinsProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Characterization of the Fast and Slow Reversible Components of Non-Photochemical Quenching in Isolated Pea Thylakoids by Picosecond Time-Resolved Chl…

1999

The fast and slow reversible components of non-photochemical chlorophyll fluorescence quenching commonly assigned to the qE and the qI mechanism have been studied in isolated pea thylakoids which were prepared from leaves after a moderate photoinhibitory treatment. Chlorophyll fluorescence decays were measured at picosecond resolution and analyzed on the basis of the heterogeneous exciton/radical pair equilibrium model. Our results show that the fast reversible non-photochemical quenching is completely assigned to the PS II antenna and is related to zeaxanthin. The slow reversible qI type quenching is located at the PS II reaction center and involves enhanced nonradiative decay of the prima…

ChlorophyllPhotosynthetic reaction centrePhotoinhibitionQuenching (fluorescence)ChemistryNon-photochemical quenchingPeasPhotochemistryBiochemistryKineticsSpectrometry FluorescencePicosecondExcited stateThylakoidChlorophyll fluorescencePlant ProteinsBiochemistry
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The Folding State of the Lumenal Loop Determines the Thermal Stability of Light-Harvesting Chlorophyll a/b Protein

2004

The major light-harvesting protein of photosystem II (LHCIIb) is the most abundant chlorophyll-binding protein in the thylakoid membrane. It contains three membrane-spanning alpha helices; the first and third one closely interact with each other to form a super helix, and all three helices bind most of the pigment cofactors. The protein loop domains connecting the alpha helices also play an important role in stabilizing the LHCIIb structure. Single amino acid exchanges in either loop were found to be sufficient to significantly destabilize the complex assembled in vitro [Heinemann, B., and Paulsen, H. (1999) Biochemistry 38, 14088-14093. Mick, V., Eggert, K., Heinemann, B., Geister, S., and…

ChlorophyllProtein DenaturationProtein FoldingPhotosystem IILight-Harvesting Protein ComplexesBiochemistryProtein structureTrypsinPlant Proteinschemistry.chemical_classificationChemistryChlorophyll AHydrolysisPeasTemperaturePhotosystem II Protein ComplexSodium Dodecyl SulfateProtein Structure TertiaryAmino acidKineticsCrystallographyAmino Acid SubstitutionMembrane proteinThylakoidHelixBiophysicsElectrophoresis Polyacrylamide GelProtein foldingAlpha helixBiochemistry
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The Light-Harvesting Chlorophyll a/b Complex Can Be Reconstituted in Vitro from Its Completely Unfolded Apoprotein

2003

The major light-harvesting chlorophyll a/b protein (LHCIIb) of higher plants is one of the few membrane proteins that can be refolded in vitro. During folding, the apoprotein is assembled with pigments to form a structurally authentic and functional pigment--protein complex. All reconstitution procedures used so far include solubilization of the apoprotein in sodium dodecyl sulfate (SDS) where the protein adopts approximately half of its alpha-helical folding present in the native structure. This paper shows that this preformed alpha-helix is not a prerequisite for LHCIIb folding in vitro. The apoprotein can also be reconstituted starting from a solution in guanidinium hydrochloride (Gnd) w…

ChlorophyllProtein FoldingChlorophyll ACircular DichroismPhotosynthetic Reaction Center Complex ProteinsKineticsLight-Harvesting Protein Complexesfood and beveragesBiochemistryFluorescenceIn vitroFolding (chemistry)B vitaminschemistry.chemical_compoundPigmentSpectrometry FluorescenceBiochemistrychemistryMembrane proteinvisual_artvisual_art.visual_art_mediumSodium dodecyl sulfateApoproteinsBiochemistry
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Evaluation of enantioselective binding of antihistamines to human serum albumin by ACE.

2007

The drug binding to plasma and tissue proteins is a fundamental factor in determining the overall pharmacological activity of a drug. HSA, together with alpha(1)-acid glycoprotein, are the most important plasma proteins, which act as drug carriers, with implications on the pharmacokinetic of drugs. Among plasma proteins, HSA possesses the highest enantioselectivity. In this paper, a new methodology for the study of enantiodifferentiation of chiral drugs with HSA is developed and applied to evaluate the possible enantioselective binding of four antihistamines: brompheniramine, chlorpheniramine, hydroxyzine and orphenadrine to HSA. This study includes the determination of affinity constants o…

ChlorpheniramineClinical BiochemistryPlasma protein bindingPharmacologyBiochemistryAnalytical ChemistryPharmacokineticsOrphenadrinemedicineOrphenadrineHumansSerum AlbuminDrug CarriersChromatographyBinding SitesChemistryBiological activityStereoisomerismBrompheniramineHuman serum albuminBrompheniraminebody regionsHydroxyzineembryonic structuresHistamine H1 AntagonistsEnantiomerDrug carriermedicine.drugProtein BindingElectrophoresis
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Cr(VI) sorption by intact and dehydrated Candida utilis cells in the presence of other metals

2002

This study examined the Cr(VI), Cu(II), Zn(II), Cd(II), Pb(II) sorption by intact and dehydrated Candida utilis cells. The anion [Cr2O7]2− and cation Me2+ sorption kinetics was investigated in both single- and dual-metal situations. Uptake of chromate anions occurred much more slowly singularly than with metal cations. A combination of Pb or Cu and chromate anions gave a synergistic effect for Cr(VI) sorption, but not Cd and Zn, which inhibited Cr(VI) sorption by dehydrated cells. The use of alcian blue to occupy maximum vacant adsorption sites on the cell surface unexpectedly did not influence further adsorption of Me2+. Metal uptake by C. utilis was 7 mg (135 μM) Cr, 23 mg (362 μM) Cu, 39…

Chromate conversion coatingChemistryMetal ions in aqueous solutionInorganic chemistrySorption kineticsBioengineeringHeavy metalsSorptionApplied Microbiology and BiotechnologyBiochemistryIonMetalAdsorptionvisual_artvisual_art.visual_art_mediumProcess Biochemistry
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TFIIH Operates through an Expanded Proximal Promoter To Fine-Tune c-myc Expression

2004

A continuous stream of activating and repressing signals is processed by the transcription complex paused at the promoter of the c-myc proto-oncogene. The general transcription factor IIH (TFIIH) is held at promoters prior to promoter escape and so is well situated to channel the input of activators and repressors to modulate c-myc expression. We have compared cells expressing only a mutated p89 (xeroderma pigmentosum complementation group B [XPB]), the largest TFIIH subunit, with the same cells functionally complemented with the wild-type protein (XPB/wt-p89). Here, we show structural, compositional, and functional differences in transcription complexes between XPB and XPB/wt-89 cells at t…

Chromatin ImmunoprecipitationDNA ComplementaryCell SurvivalUltraviolet RaysBlotting WesternGreen Fluorescent ProteinsGene ExpressionRepressorCellular homeostasisBiologyTransfectionModels BiologicalProto-Oncogene MasProto-Oncogene Proteins c-mycTranscription Factors TFIIRibonucleasesPotassium PermanganateTranscription (biology)HumansRNA MessengerPromoter Regions GeneticMolecular BiologyModels GeneticGeneral transcription factorCell CycleGenetic Complementation TestDNA HelicasesPromoterCell BiologyFibroblastsFlow CytometryMolecular biologyDNA-Binding ProteinsKineticsTranscription Factor TFIIHMicroscopy FluorescenceMutationTranscription preinitiation complexTranscription factor II HTranscription Factor TFIIHPlasmidsMolecular and Cellular Biology
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Partial vinylphenol reductase purification and characterization from Brettanomyces bruxellensis

2008

International audience; Brettanomyces is the major microbial cause for wine spoilage worldwide and causes significant economic losses. The reasons are the production of ethylphenols that lead to an unpleasant taint described as 'phenolic odour'. Despite its economic importance, Brettanomyces has remained poorly studied at the metabolic level. The origin of the ethylphenol results from the conversion of vinylphenols in ethylphenol by Brettanomyces hydroxycinnamate decarboxylase. However, no information is available on the vinylphenol reductase responsible for the conversion of vinylphenols in ethylphenols. In this study, a vinylphenol reductase was partially purified from Brettanomyces bruxe…

Chromatography GasBrettanomycesMolecular Sequence DataVINYLPHENOL REDUCTASEBrettanomyces bruxellensisWineReductaseMicrobiology[ CHIM ] Chemical SciencesFungal Proteins03 medical and health sciencesHydrolysisOpen Reading FramesPhenolsOxidoreductaseGenetics[CHIM]Chemical SciencesAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classificationWineVOLATILE PHENOL0303 health sciencesbiology030306 microbiologyChemistryGuaiacolTemperatureBRETTANOMYCESHydrogen-Ion Concentrationbiology.organism_classificationNADAmino acidMolecular WeightKineticsEnzymeBiochemistryDETERIORATION MICROBIENNESaccharomycetalesBRUTTANOMYCES BRUXELLENSISFood MicrobiologyElectrophoresis Polyacrylamide GelOxidoreductases
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Molecular organization via ionic interactions at interfaces. 1. Monolayers and LB films of cyclic bisbipyridinium tetracations and dimyristoylphospha…

1993

ChromatographyAqueous solutionChemical structureKineticsPhospholipidIonic bondingSurfaces and InterfacesCondensed Matter PhysicsSurface pressurechemistry.chemical_compoundchemistryChemical engineeringMonolayerElectrochemistryDimyristoylphosphatidic acidGeneral Materials ScienceSpectroscopyLangmuir
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