Search results for "LIGHT"

showing 10 items of 3575 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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Sun-induced fluorescence - a new probe of photosynthesis: First maps from the imaging spectrometer HyPlant.

2015

Variations in photosynthesis still cause substantial uncertainties in predicting photosynthetic CO2 uptake rates and monitoring plant stress. Changes in actual photosynthesis that are not related to greenness of vegetation are difficult to measure by reflectance based optical remote sensing techniques. Several activities are underway to evaluate the sun-induced fluorescence signal on the ground and on a coarse spatial scale using space-borne imaging spectrometers. Intermediate-scale observations using airborne-based imaging spectroscopy, which are critical to bridge the existing gap between small-scale field studies and global observations, are still insufficient. Here we present the first …

Chlorophyllinduced fluorescencesunImaging spectrometer2306 Global and Planetary ChangeFluorescence2300 General Environmental SciencePhotosynthesiEnvironmental ChemistryAirborne measurement910 Geography & travelSpectral resolutionPhotosynthesisAbsorption (electromagnetic radiation)Spectroscopyairborne measurementsChlorophyll fluorescenceGeneral Environmental ScienceRemote sensingGlobal and Planetary ChangeSpectrometerEcology2300Remote sensingImaging spectroscopyVegetation monitoringFLEXImaging spectroscopy10122 Institute of GeographyGEO/10 - GEOFISICA DELLA TERRA SOLIDASpectrometry FluorescenceSun-induced fluorescence2304 Environmental ChemistryHyPlantRemote Sensing TechnologySunlightEnvironmental scienceSpatial variabilityChlorophyll fluorescence2303 EcologyGlobal change biology
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The intensification of absorbance changes in leaves by light-dispersion

1979

In dispersive samples, like leaves, the absorbance of pigments is intensified. The intensification is due to a longer optical path through the dispersive sample. However, in chloroplast suspensions the optical path is not much longer than in clear solutions. The factor of intensification β (=the lengthening of the optical path) is calculated by comparing the absorbance of leaves and the absorbance of chloroplast suspensions with equal pigment-content. This method also includes the influence of possible sieve effects which could decrease absorbance. The measurements are carried out with high- and low-light leaves of different thickness and pigment content. The intensification of absorbance w…

ChloroplastAbsorbanceCytochrome fPigmentChromatographyChemistryvisual_artLight dispersionGeneticsAnalytical chemistryvisual_art.visual_art_mediumsense organsPlant SciencePlanta
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Calvin-Benson Cycle

2015

A carbon dioxide fixation pathway where a molecule of CO2 condenses with a 5-C compound (ribulose 1,5-bisphosphate) to yield two molecules of a 3-C compound (3-phosphoglycerate). These 3-C molecules serve both as precursors for biosynthesis and, through a cyclic series of enzymatic reactions, to regenerate the 5-C molecule necessary for the first carboxylating step (Fig. 1). The pathway is present in several bacterial lineages (e.g., cyanobacteria), and its acquisition by eukaryotic cells (chloroplast in algae and plants) was through the endosymbiotic association with ancient cyanobacteria.

ChloroplastCyanobacteriachemistry.chemical_compoundbiologyAlgaeBiosynthesisBiochemistryChemistryRibuloseCarbon fixationLight-independent reactionsbiology.organism_classificationEnzyme catalysis
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