Search results for "Pigments"

showing 10 items of 135 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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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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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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Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

2005

A new potential light-harvesting protein, named Lhca5, was recently detected in higher plants. Because of the low amount of Lhca5 in thylakoid membranes, the isolation of a native Lhca5 pigment-protein complex has not been achieved to date. Therefore, we used in vitro reconstitution to analyze whether Lhca5 binds pigments and is actually an additional light-harvesting protein. By this approach we could demonstrate that Lhca5 binds pigments in a unique stoichiometry. Analyses of pigment requirements for light-harvesting complex formation by Lhca5 revealed that chlorophyll b is the only indispensable pigment. Fluorescence measurements showed that ligated chlorophylls and carotenoids are arran…

ChlorophyllChlorophyll bPigment bindingArabidopsisLight-Harvesting Protein Complexesmacromolecular substancesBiologyPhotosystem IBiochemistryFluorescencechemistry.chemical_compoundProtein structureProtein Structure QuaternaryMolecular BiologyPhotosystemPhotosystem I Protein ComplexArabidopsis ProteinsPigments BiologicalCell BiologyCarotenoidsFluorescenceBiochemistrychemistryThylakoidChlorophyll Binding ProteinsChlorophyll Binding ProteinsDimerizationJournal of Biological Chemistry
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The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b c…

2008

AbstractThe major chlorophyll (Chl) a/b complexes of photosystem II (LHCIIb), in addition to their primary light-harvesting function, play key roles in the organization of the granal ultrastructure of the thylakoid membranes and in various regulatory processes. These functions depend on the structural stability and flexibility of the complexes. The lumenal side of LHCIIb is exposed to broadly variable pH environments, due to the build-up and decay of the pH gradient during photosynthesis. Therefore, the negatively charged amino acids in the lumenal loop might be of paramount importance for adjusting the structure and functions of LHCIIb. In order to clarify the structural roles of these res…

ChlorophyllCircular dichroismPhotosystem IIPigment bindingMolecular ConformationBiophysicsPhotosynthesisBiochemistryMajor light-harvesting a/b complex of photosystem IILow pHAmino AcidsSpectroscopyPhotosystemchemistry.chemical_classificationChemistryCircular DichroismPhotosystem II Protein ComplexPigments BiologicalCell BiologyHydrogen-Ion ConcentrationAmino acidCrystallographyB vitaminsMutagenesisThylakoidBiophysicsElectrophoresis Polyacrylamide GelProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Boronic Acids of Pharmaceutical Importance Affect the Growth and Photosynthetic Apparatus of Cyanobacteria in a Dose-Dependent Manner

2020

The dynamic increase in the commercial application of antimicrobial derivatives of boronic acids, and potential impact of their presence in aquatic systems, supports the necessity to study the toxicity of these substances towards microorganisms of crucial meaning in the environment. One example of the mentioned derivatives is tavaborole (5-fluoro-substituted benzoxaborole), a pharmaceutical agent with antifungal activity. Cyanobacteria were used as model organisms, which are photoautotrophic prokaryotes, as representative aquatic bacteria and photoautotrophs associated with the plant kingdom. To the best of our knowledge, we investigated this issue for the first time. In order to recognize …

ChlorophyllCyanobacteriaHealth Toxicology and MutagenesisMicroorganismlcsh:Medicinebactericidal activitypharmaceuticalsToxicologyPhotosynthesisaryl boronic acids01 natural sciencescyanobacteriaArticle03 medical and health scienceschemistry.chemical_compoundFood sciencephotosynthetic pigmentsPhotosynthesisCarotenoidchemistry.chemical_classification0303 health sciencesDose-Response Relationship Drugbiology010405 organic chemistry030306 microbiologyChemistryPhycobiliproteinlcsh:RAntimicrobialbiology.organism_classificationBoronic AcidsHalophile0104 chemical sciencesChlorophyllToxins
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Carotenoid binding sites in LHCIIb

2000

The major light-harvesting complex of photosystem II can be reconstituted in vitro from its bacterially expressed apoprotein with chlorophylls a and b and neoxanthin, violaxanthin, lutein, or zeaxanthin as the only xanthophyll. Reconstitution of these one-carotenoid complexes requires low-stringency conditions during complex formation and isolation. Neoxanthin complexes (containing 30–50% of the all-trans isomer) disintegrate during electrophoresis, exhibit a largely reduced resistance against proteolytic attack; in addition, energy transfer from Chl b to Chl a is easily disrupted at elevated temperature. Complexes reconstituted in the presence of either zeaxanthin or lutein contain nearly …

ChlorophyllLuteinPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesXanthophyllsBiologyBinding CompetitiveBiochemistrySubstrate SpecificityLight-harvesting complexchemistry.chemical_compoundNeoxanthinZeaxanthinsTrypsinProtein PrecursorsCarotenoidPlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll ALuteinPhotosystem II Protein Complexfood and beveragesPigments BiologicalPlantsbeta CaroteneCarotenoidseye diseasesZeaxanthinEnergy TransferchemistryBiochemistryXanthophyllElectrophoresis Polyacrylamide GelApoproteinsViolaxanthinEuropean Journal of Biochemistry
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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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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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Modulation of the growth and metabolic response of cyanobacteria by the multifaceted activity of naringenin

2017

The interactions between the plant-derived bioflavonoid, naringenin, and prokaryotic microalgae representatives (cyanobacteria), were investigated with respect to its influence on the growth and metabolic response of these microorganisms. To achieve reliable results, the growth of cyanobacteria was determined based on measurements of chlorophyll content, morphological changes were assessed through microscopic observations, and the chemical response of cells was determined using liquid and gas chromatography (HPLC; GC-FID). The results show that micromolar levels of naringenin stimulated the growth of cyanobacteria. Increased growth was observed for halophilic strains at naringenin concentra…

ChlorophyllPigments0301 basic medicineCyanobacteriaNaringeninExopolysaccharidesChloroplastsMicroorganismCellGlycobiologyMarine and Aquatic Scienceslcsh:MedicineFresh WaterPlant ScienceBiochemistrychemistry.chemical_compoundElectron MicroscopyNostoclcsh:ScienceLiquid ChromatographyMicroscopyMultidisciplinarybiologyChemistryChromatographic Techniquesfood and beveragesHalophilemedicine.anatomical_structureBiochemistryFlavanonesPhysical SciencesScanning Electron MicroscopyCellular Structures and OrganellesCellular TypesResearch ArticleFreshwater EnvironmentsChromatography GasPlant Cell BiologyMaterials Science030106 microbiologyCyanobacteriaResearch and Analysis MethodsCell wallExcretion03 medical and health sciencesPolysaccharidesPlant CellsmedicineMaterials by AttributeBacteriaOrganic PigmentsEcology and Environmental Scienceslcsh:ROrganismsBiology and Life SciencesAquatic EnvironmentsCell Biologybiology.organism_classificationAnabaenaHigh Performance Liquid Chromatography030104 developmental biologyEarth Scienceslcsh:QBacteriaChromatography LiquidNostoc muscorumPLOS ONE
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