Search results for "Complex."

showing 10 items of 5824 documents

Chlorophyll b is involved in long-wavelength spectral properties of light-harvesting complexes LHC I and LHC II.

2001

AbstractChlorophyll (Chl) molecules attached to plant light-harvesting complexes (LHC) differ in their spectral behavior. While most Chl a and Chl b molecules give rise to absorption bands between 645 nm and 670 nm, some special Chls absorb at wavelengths longer than 700 nm. Among the Chl a/b-antennae of higher plants these are found exclusively in LHC I. In order to assign this special spectral property to one chlorophyll species we reconstituted LHC of both photosystem I (Lhca4) and photosystem II (Lhcb1) with carotenoids and only Chl a or Chl b and analyzed the effect on pigment binding, absorption and fluorescence properties. In both LHCs the Chl-binding sites of the omitted Chl species…

Chlorophyll bChlorophyllPhotosystem IIPigment bindingPhotosynthetic Reaction Center Complex ProteinsBiophysicsLight-Harvesting Protein ComplexesPhotosystem IPhotochemistryBiochemistryAbsorptionLight-harvesting complexReconstitutionchemistry.chemical_compoundSolanum lycopersicumStructural BiologySpinacia oleraceaGeneticsChlorophyll bindingCentrifugation Density GradientMolecular BiologyChlorophyll fluorescenceLong-wavelength chlorophyllBinding SitesPhotosystem I Protein ComplexChemistryChlorophyll ATemperaturePhotosystem II Protein ComplexLight-harvesting complexes of green plantsCell BiologyPigments BiologicalPlant LeavesSpectrometry FluorescenceLight-harvesting complexChlorophyll fluorescenceChlorophyll bindingProtein BindingFEBS letters
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Random mutations directed to transmembrane and loop domains of the light-harvesting chlorophyll a/b protein: impact on pigment binding.

1999

The major light-harvesting complex of photosystem II (LHCII) can be reconstituted in vitro by folding its bacterially expressed apoprotein, Lhcb, in detergent solution in the presence of chlorophylls and carotenoids. To compare the impact of alpha-helical transmembrane domains and hydrophilic loop domains of the apoprotein on complex formation and stability, we introduced random mutations into a segment of the protein comprising the stromal loop, the third (C-proximal) transmembrane helix, and part of the amphipathic helix in the C-terminal domain. The mutant versions of Lhcb were screened for the loss of their ability to form stable LHCII upon reconstitution in vitro. Most steps during the…

Chlorophyll bChlorophyllProtein FoldingPigment bindingMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureChlorophyll bindingAmino Acid SequencePeptide sequencePeasMembrane ProteinsPhotosystem II Protein ComplexCarotenoidsTransmembrane proteinProtein Structure TertiaryTransmembrane domainSpectrometry FluorescencechemistryBiochemistryEnergy TransferMutationMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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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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Comparative analysis of the composition of two chlorophyll-b-containing light-harvesting complexes.

1990

The major light-harvesting complexes from Mantoniella squamata (Prasinophyceae) and from Chlorella fusca (Chlorophyceae) were analyzed with respect to polypeptide composition and pigmentation. It was found that the polypeptides of Mantoniella are smaller than those of Chlorella and bind twice the amount of pigment. We assume that the amount of pigment per polypeptide is of ecological as well as of taxonomical importance.

Chlorophyll bbiologyPrasinophyceaeChlorophyceaePlant Sciencebiology.organism_classificationLight-harvesting complexChlorellachemistry.chemical_compoundPigmentAlgaechemistryMantoniellavisual_artBotanyvisual_art.visual_art_mediumGeneticssense organsPlanta
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Effects of chlorophyll a, chlorophyll b, and xanthophylls on the in vitro assembly kinetics of the major light-harvesting chlorophyll a/b complex, LH…

2001

The major light-harvesting chlorophyll a/b complex (LHCIIb) of photosystem II in higher plants can be reconstituted with pigments in lipid-detergent micelles. The pigment-protein complexes formed are functional in that they perform efficient internal energy transfer from chlorophyll b to chlorophyll a. LHCIIb formation in vitro, can be monitored by the appearance of energy transfer from chlorophyll b to chlorophyll a in time-resolved fluorescence measurements. LHCIIb is found to form in two apparent kinetic steps with time constants of about 30 and 200 seconds. Here we report on the dependence of the LHCIIb formation kinetics on the composition of the pigment mixture used in the reconstitut…

Chlorophyll bchemistry.chemical_classificationChlorophyll afood and beveragesLight-harvesting complexes of green plantsPhotochemistrychemistry.chemical_compoundB vitaminschemistryNeoxanthinStructural BiologyChlorophyllXanthophyllChlorophyll bindingMolecular BiologyJournal of Molecular Biology
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Rigid versus Flexible Protein Matrix: Light-Harvesting Complex II Exhibits a Temperature-Dependent Phonon Spectral Density

2018

Dynamics-function correlations are usually inferred when molecular mobility and protein function are simultaneously impaired at characteristic temperatures or hydration levels. In this sense, excitation energy transfer in the photosynthetic light-harvesting complex II (LHC II) is an untypical example because it remains fully functional even at cryogenic temperatures relying mainly on interactions of electronic states with protein vibrations. Here, we study the vibrational and conformational protein dynamics of monomeric and trimeric LHC II from spinach using inelastic neutron scattering (INS) in the temperature range of 20-305 K. INS spectra of trimeric LHC II reveal a distinct vibrational …

Chlorophyll0301 basic medicineMaterials sciencePhononLight-Harvesting Protein Complexes010402 general chemistry01 natural sciencesMolecular physicsInelastic neutron scatteringSpectral line03 medical and health sciencesSpinacia oleraceaMaterials ChemistryPhysics::Chemical PhysicsPhysical and Theoretical ChemistrySofteningQuantitative Biology::BiomoleculesProtein dynamicsAnharmonicityTemperaturefood and beveragesAtmospheric temperature rangeProtein Structure Tertiary0104 chemical sciencesSurfaces Coatings and FilmsNeutron Diffraction030104 developmental biologyEnergy TransferExcitationThe Journal of Physical Chemistry B
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A field study on solar-induced chlorophyll fluorescence and pigment parameters along a vertical canopy gradient of four tree species in an urban envi…

2013

Abstract: To better understand the potential uses of vegetation indices based on the sun-induced upward and downward chlorophyll fluorescence at leaf and at canopy scales, a field study was carried out in the city of Valencia (Spain). Fluorescence yield (FY) indices were derived for trees at different traffic intensity locations and at three canopy heights. This allowed investigating within-tree and between-tree variations of FY indices for four tree species. Several FY indices showed a significant (p < 0.05) and important effect of tree location for the species Morus alba (white mulberry) and Phoenix canariensis (Canary Island date palm). The upward FY parameters of M. alba, and the upward…

ChlorophyllCanopyEnvironmental EngineeringPhotosynthesisAtmospheric sciencesFiresFluorescenceTreesLight-harvesting complexchemistry.chemical_compoundBotanyEnvironmental ChemistryCitiesWaste Management and DisposalChlorophyll fluorescenceBiologyAir PollutantsbiologyVegetationbiology.organism_classificationPollutionPlant LeavesChemistrychemistrySpainPhoenix canariensisChlorophyllEnvironmental scienceParticulate MatterShadingEnvironmental MonitoringThe science of the total environment
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Excitonic energy level structure and pigment-protein interactions in the recombinant water-soluble chlorophyll protein. II. Spectral hole-burning exp…

2011

Persistent spectral hole burning at 4.5 K has been used to investigate the excitonic energy level structure and the excited state dynamics of the recombinant class-IIa water-soluble chlorophyll-binding protein (WSCP) from cauliflower. The hole-burned spectra are composed of four main features: (i) a narrow zero-phonon hole (ZPH) at the burn wavelength, (ii) a number of vibrational ZPHs, (iii) a broad low-energy hole at ~665 and ~683 nm for chlorophyll b- and chlorophyll a-WSCP, respectively, and (iv) a second satellite hole at ~658 and ~673 nm for chlorophyll b- and chlorophyll a-WSCP, respectively. The doublet of broad satellite holes is assigned to an excitonically coupled chlorophyll dim…

ChlorophyllChlorophyll aExcitonAnalytical chemistryLight-Harvesting Protein ComplexesElectronsBrassicaVibrationSpectral linechemistry.chemical_compoundMaterials ChemistryPhysical and Theoretical ChemistryPhysics::Biological PhysicsChlorophyll AWaterFluorescenceRecombinant ProteinsSurfaces Coatings and FilmsWavelengthSpectrometry FluorescencechemistryExcited stateChlorophyllSpectral hole burningThermodynamicsAtomic physicsThe journal of physical chemistry. B
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Pigment binding of photosystem I light-harvesting proteins.

2002

Light-harvesting complexes (LHC) of higher plants are composed of at least 10 different proteins. Despite their pronounced amino acid sequence homology, the LHC of photosystem II show differences in pigment binding that are interpreted in terms of partly different functions. By contrast, there is only scarce knowledge about the pigment composition of LHC of photosystem I, and consequently no concept of potentially different functions of the various LHCI exists. For better insight into this issue, we isolated native LHCI-730 and LHCI-680. Pigment analyses revealed that LHCI-730 binds more chlorophyll and violaxanthin than LHCI-680. For the first time all LHCI complexes are now available in t…

ChlorophyllChlorophyll aPhotosystem IIPigment bindingPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyXanthophyllsPhotosystem IBiochemistrychemistry.chemical_compoundPigmentSolanum lycopersicumMolecular BiologyP700Binding SitesPhotosystem I Protein ComplexChlorophyll Afood and beveragesPhotosystem II Protein ComplexCell BiologyPigments Biologicalbeta CarotenePlant LeavesSpectrometry FluorescencechemistryBiochemistryChlorophyllvisual_artvisual_art.visual_art_mediumViolaxanthinThe Journal of biological chemistry
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