Search results for " Spectroscopy"

showing 10 items of 6851 documents

Pigment−Pigment and Pigment−Protein Interactions in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower

2007

Plants contain water-soluble chlorophyll-binding proteins (WSCPs) that function neither as antennas nor as components of light-induced electron transfer of photosynthesis but are likely constituents of regulatory protective pathways in particular under stress conditions. This study presents results on the spectroscopic properties of recombinant WSCP from cauliflower reconstituted with chlorophyll b (Chl b) alone or with mixtures of Chl a and Chl b. Two types of experiments were performed: (a) measurements of stationary absorption spectra at 77 and 298 K and CD spectra at 298 K and (b) monitoring of laser flash-induced transient absorption changes with a resolution of 200 fs in the time doma…

Chlorophyll bCircular dichroismAbsorption spectroscopyCircular DichroismLasersDimerKineticsLight-Harvesting Protein ComplexesBrassicaPigments BiologicalRecombinant ProteinsSurfaces Coatings and FilmsKineticschemistry.chemical_compoundCrystallographyElectron transferchemistryUltrafast laser spectroscopyChlorinMaterials ChemistryLinear Energy TransferSpectrophotometry UltravioletPhysical and Theoretical ChemistryThe Journal of Physical Chemistry B
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Characterisation of Chlorophyll a and Chlorophyll b Monomers in Various Solvent Environments with Ultrafast Spectroscopy

1998

In photosynthesis the energy from the sun is captured by light harvesting chlorophyll pigments and converted to stable chemical energy, by the photochemical reaction center. Photosynthetic energy transfer in the antenna systems of green plants has previously been studied by ultrafast time resolved spectroscopy. The characteristics of the chlorophyll pigments itself is important to study in order to understand the dynamics on a femtosecond timescale. One way to study the energy transfer is to use transient absorption spectroscopy and follow the increase or decrease in the transient absorption signal with time (1). Another way to study the energy transfer is to monitor the change in dichroism…

Chlorophyll bPhysics::Biological Physics0303 health sciencesChlorophyll aMaterials scienceDichroism010402 general chemistryPhotochemistry7. Clean energy01 natural sciences0104 chemical sciencesLight-harvesting complex03 medical and health scienceschemistry.chemical_compoundchemistryChlorophyllUltrafast laser spectroscopyTime-resolved spectroscopySpectroscopy030304 developmental biology
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Accessibility of Protein-Bound Chlorophylls Probed by Dynamic Electron Polarization

2018

The possibility to probe the accessibility of sites of proteins represents an important point to explore their interactions with specific substrates in solution. The dynamic electron polarization of nitroxide radicals induced by excited triplet states of organic molecules is a phenomenon that is known to occur in aqueous solutions. The interaction within the radical-triplet pair causes a net emissive dynamic electron polarization of the nitroxide radical, that can be detected by means of time-resolved electron paramagnetic resonance (TR-EPR) spectroscopy. We have exploited this effect to prove the accessibility of chlorophylls bound to a protein, namely, the water-soluble chlorophyll protei…

Chlorophyll0301 basic medicineNitroxide mediated radical polymerizationFree RadicalsRadicalElectron010402 general chemistry01 natural scienceslaw.inventionElectron Transport03 medical and health scienceslawGeneral Materials SciencePhysical and Theoretical ChemistryPolarization (electrochemistry)Electron paramagnetic resonanceSpectroscopyChemistryElectron Spin Resonance SpectroscopyProteinsChlorophyll; Electron Spin Resonance Spectroscopy; Electron Transport; Free Radicals; Nitrogen Oxides; Protein Binding; Proteins0104 chemical sciences030104 developmental biologyChemical physicsExcited stateNitrogen OxidesProtein BindingMacromoleculeThe Journal of Physical Chemistry Letters
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Filling the “green gap” of the major light-harvesting chlorophyll a/b complex by covalent attachment of Rhodamine Red

2009

AbstractThe major light-harvesting chlorophyll a/b complex (LHCII) greatly enhances the efficiency of photosynthesis in green plants. Recombinant LHCII can be assembled in vitro from its denatured, bacterially expressed apoprotein and plant pigments. This makes it an interesting candidate for biomimetic light-harvesting in photovoltaic applications. Due to its almost 20 pigments bound per apoprotein, LHCII absorbs efficiently in the blue and red spectral domains of visible light but less efficiently in the green domain, the so-called “green gap” in its absorption spectrum. Here we present a hybrid complex of recombinant LHCII with organic dyes that add to LHCII absorption in the green spect…

ChlorophyllLHCIIProtein FoldingFRET (Förster resonance energy transfer)Chlorophyll aAbsorption spectroscopyBiophysicsPhotosynthesisPhotochemistryBiochemistryRhodamineLight-harvesting complexchemistry.chemical_compoundPhotosynthesisFluorescent DyesRhodaminesChlorophyll Afood and beveragesSite-specific labelingCell BiologyMaleimide dyeB vitaminsSolar spectrumchemistryChlorophyllVisible spectrumBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Hierarchical Self-Organization of Perylene Bisimide–Melamine Assemblies to Fluorescent Mesoscopic Superstructures

2000

A series of three perylene tetracarboxylic acid bisimide dyes 3a-c bearing phenoxy substituents at the four bay positions of the perylene core were synthesized and their complexation behavior to complementary ditopic dialkyl melamines 8a-c was investigated. Binding constants and Gibbs binding energies for the hydrogen bonds between the imide and the complementary melamine moiety have been determined in several solvents by NMR and UV/Vis titration experiments with monotopic model compounds 5 and 9. The effects of the solvent polarity and specific solvent-solute interactions on the degree of polymerization of (3 x 8)n are discussed, and a general formula to estimate the chain length of [AA-BB…

ChlorophyllMagnetic Resonance SpectroscopyLightPolymersMolecular ConformationSupramolecular chemistryDegree of polymerizationImidesPhotochemistryFluorescenceCatalysischemistry.chemical_compoundNon-covalent interactionsPerylenechemistry.chemical_classificationMicroscopy ConfocalTriazinesHydrogen bondOrganic ChemistryOptical polarizationPolymerGeneral ChemistrySolutionsSupramolecular polymersMicroscopy ElectronchemistrySpectrophotometry UltravioletPeryleneChemistry – A European Journal
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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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Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
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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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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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