Search results for "complexes"

showing 10 items of 875 documents

Evidence for two spectroscopically different dimers of light-harvesting complex I from green plants

2000

A preparation consisting of isolated dimeric peripheral antenna complexes from green plant photosystem I (light-harvesting complex I or LHCI) has been characterized by means of (polarized) steady-state absorption and fluorescence spectroscopy at low temperatures. We show that this preparation can be described reasonably well by a mixture of two types of dimers. In the first dimer about 10% of all Q(y)() absorption of the chlorophylls arises from two chlorophylls with absorption and emission maxima at about 711 and 733 nm, respectively, whereas in the second about 10% of the absorption arises from two chlorophylls with absorption and emission maxima at about 693 and 702 nm, respectively. The…

ChlorophyllP700Photosystem IIPhotosystem I Protein ComplexChemistryDimerCircular DichroismPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexPhotochemistryPhotosystem IBiochemistryZea maysFluorescence spectroscopychemistry.chemical_compoundSpectrometry FluorescenceLight harvesting complex ISpectrophotometryAbsorption (chemistry)Protein Structure QuaternaryDimerization
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Light-harvesting chlorophyll protein (LHCII) drives electron transfer in semiconductor nanocrystals

2017

Type-II quantum dots (QDs) are capable of light-driven charge separation between their core and the shell structures; however, their light absorption is limited in the longer-wavelength range. Biological light-harvesting complex II (LHCII) efficiently absorbs in the blue and red spectral domains. Therefore, hybrid complexes of these two structures may be promising candidates for photovoltaic applications. Previous measurements had shown that LHCII bound to QD can transfer its excitation energy to the latter, as indicated by the fluorescence emissions of LHCII and QD being quenched and sensitized, respectively. In the presence of methyl viologen (MV), both fluorescence emissions are quenched…

ChlorophyllParaquatPhotosynthetic reaction centreMaterials scienceAbsorption spectroscopyLight-Harvesting Protein ComplexesBiophysics02 engineering and technology010402 general chemistryPhotochemistry01 natural sciencesBiochemistryElectron TransportLight-harvesting complexElectron transferQuantum DotsUltrafast laser spectroscopyFluorescence Resonance Energy TransferAction spectrumPeasPhotosystem II Protein ComplexCell Biology021001 nanoscience & nanotechnologyFluorescence0104 chemical sciencesSemiconductorsQuantum dotNanoparticles0210 nano-technologyBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Expression of a higher plant light-harvesting chlorophyll a/b-binding protein in Synechocystis sp. PCC 6803

1999

A chimeric lhcb gene, coding for Lhcb, a higher plant chlorophyll a/b-binding light-harvesting complex of photosystem II (LHCII), was constructed using the Synechocystis sp. PCC 6803 psbA3 promoter and a modified lhcb gene from pea. This construct drives synthesis of full-length, mature Lhcb under the control of the strong psbA3 promoter that usually drives expression of the D1 protein of photosystem II. This chimeric gene was transformed into a photosystem I-less/chlL(-) Synechocystis sp. PCC 6803 strain that is unable to synthesize chlorophyll in darkness. In the resulting strain, a high level of lhcb transcript was detected and transcript accumulation was enhanced by addition of exogenou…

ChlorophyllPhotosystem IIRecombinant Fusion ProteinsPhotosynthetic Reaction Center Complex ProteinsPigment bindingMutantLight-Harvesting Protein ComplexesGene ExpressionChimeric geneBiologyCyanobacteriaBiochemistrychemistry.chemical_compoundTransformation GeneticIntegral membrane proteinChromatography High Pressure LiquidPlant ProteinsPhotosystemModels GeneticPhotosystem I Protein ComplexPhotosystem II Protein ComplexPigments BiologicalSpectrometry FluorescenceBiochemistrychemistryThylakoidChlorophyllRNAEuropean Journal of Biochemistry
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Water soluble chlorophyll binding protein of higher plants: A most suitable model system for basic analyses of pigment–pigment and pigment–protein in…

2011

Abstract This short review paper describes spectroscopic studies on pigment–pigment and pigment–protein interactions of chlorophyll (Chl) a and b bound to the recombinant protein of class IIa water soluble chlorophyll protein (WSCP) from cauliflower. Two Chls form a strongly excitonically coupled open sandwich dimer within the tetrameric protein matrix. In marked contrast to the mode of excitonic coupling of Chl and bacterio-Chl molecules in light harvesting complexes and reaction centers of all photosynthetic organisms, the unique structural pigment array in the Chl dimer of WSCP gives rise to an upper excitonic state with a large oscillator strength. This property opens the way for thorou…

ChlorophyllPhysiologyTetrameric proteinDimerLight-Harvesting Protein ComplexesTemperatureWatermacromolecular substancesPlant SciencePlantsPhotochemistryPhotosynthesisModels BiologicalLight-harvesting complexchemistry.chemical_compoundPigmentchemistryChlorophyllvisual_artvisual_art.visual_art_mediumChlorophyll bindingMoleculeAgronomy and Crop ScienceJournal of Plant Physiology
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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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Chlamydomonas reinhardtii in the landscape of pigments.

2004

▪ Abstract  This review focuses on the biosynthesis of pigments in the unicellular alga Chlamydomonas reinhardtii and their physiological and regulatory functions in the context of information gathered from studies of other photosynthetic organisms. C. reinhardtii is serving as an important model organism for studies of photosynthesis and the pigments associated with the photosynthetic apparatus. Despite extensive information pertaining to the biosynthetic pathways critical for making chlorophylls and carotenoids, we are just beginning to understand the control of these pathways, the coordination between pigment and apoprotein synthesis, and the interactions between the activities of these…

ChlorophyllRhodopsinNuclear geneChloroplastsved/biology.organism_classification_rank.speciesLight-Harvesting Protein ComplexesProtozoan ProteinsChlamydomonas reinhardtiiPhotosynthesisModels Biologicalchemistry.chemical_compoundHemiterpenesLycopeneBiosynthesisIsomerismPentanesBotanyGeneticsButadienesAnimalsPhotosynthesisModel organismCarotenoidPlant Proteinschemistry.chemical_classificationCell Nucleusbiologyved/biologyPigments Biologicalbiology.organism_classificationCarotenoidsChloroplastOxygenCytochrome b6f ComplexchemistryBiochemistryXanthophyllPhotoreceptor Cells InvertebrateChlamydomonas reinhardtiiAnnual review of genetics
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The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression

2008

Inner nuclear membrane proteins containing a LEM (LAP2, emerin, and MAN1) domain participate in different processes, including chromatin organization, gene expression, and nuclear envelope biogenesis. In this study, we identify a robust genetic interaction between transcription export (TREX) factors and yeast Src1, an integral inner nuclear membrane protein that is homologous to vertebrate LEM2. DNA macroarray analysis revealed that the expression of the phosphate-regulated genes PHO11, PHO12, and PHO84 is up-regulated in src1Δ cells. Notably, these PHO genes are located in subtelomeric regions of chromatin and exhibit a perinuclear location in vivo. Src1 spans the nuclear membrane twice an…

Chromatin ImmunoprecipitationSaccharomyces cerevisiae ProteinsGenes FungalSaccharomyces cerevisiaeProtein Sorting SignalsBiologyArticleGenètica molecularProton-Phosphate SymportersGene Expression Regulation FungalGene expressionmedicineExpressió genèticaInner membraneNuclear proteinNuclear poreNuclear membraneResearch ArticlesNucleoplasmMembrane ProteinsNuclear ProteinsCell BiologyTelomereMolecular biologyChromatinProtein Structure TertiaryChromatinAlternative SplicingGenòmicamedicine.anatomical_structureMultiprotein ComplexesNuclear lamina
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Silica Entrapment for Significantly Stabilized, Energy-Conducting Light-Harvesting Complex (LHCII)

2014

The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants consists of a membrane protein and numerous noncovalently bound pigments that make up about one-third of the molecular mass of the pigment-protein complex. Due to this high pigment density, LHCII is potentially interesting as a light-harvesting component in synthetic constructs. However, for such applications its stability needs to be significantly improved. In this work, LHCII was dramatically stabilized by enclosing it within polymerizing colloidal silica. The entrapped LHCII stayed functional at 50 °C for up to 24 h instead of a few minutes in detergent solution and clearly showed e…

ChromatographyMolecular massChemistryColloidal silicaLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexSurfaces and InterfacesSilicon DioxideCondensed Matter PhysicsPhotosynthesisLight-harvesting complexB vitaminsPigmentPolymerizationYield (chemistry)visual_artElectrochemistryBiophysicsvisual_art.visual_art_mediumGeneral Materials ScienceSpectroscopyLangmuir
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Evaluation of molecular mass and tacticity of polyvinyl alcohol by non-equilibrium capillary electrophoresis of equilibrium mixtures of a polymer and…

2011

Non-equilibrium capillary electrophoresis of equilibrium mixtures (NECEEM) has been used to characterize polyvinyl alcohol (PVA). Commercial PVA samples with different molecular masses, from M(w)=15 up to 205 kDa, were used. According to the (13)C NMR spectra, the samples also differed in tacticity (stereoregularity). Mixtures of PVA and the anionic azo-dye Congo Red (CR) were injected in the presence of a borate buffer. The electropherograms gave a band and a peak due to the residual PVA-CR complex and the excess dye, respectively, plus a superimposed exponential decay due to the partial dissociation of the complex during migration. The stoichiometry of the PVA-CR complex, q=[monomer]/[dye…

Chromatographyintegumentary systemOrganic ChemistryElectrophoresis CapillaryCongo RedGeneral MedicineBiochemistryPolyvinyl alcoholDissociation (chemistry)Analytical ChemistryMolecular Weightchemistry.chemical_compoundElectrophoresisMonomerCapillary electrophoresischemistryStability constants of complexesPolyvinyl AlcoholTacticityBoratesSpectrophotometry UltravioletAzo CompoundsStoichiometryJournal of Chromatography A
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