Search results for "complex"

showing 10 items of 5889 documents

Inactivation of a plastid evolutionary conserved gene affects PSII electron transport, life span and fitness of tobacco plants

2007

Chloroplasts contain a plastoquinone-NADH-oxidoreductase (Ndh) complex involved in protection against stress and the maintenance of cyclic electron flow. Inactivation of the Ndh complex delays the development of leaf senescence symptoms. Chlorophyll a fluorescence measurements, blue native gel electrophoresis, immunodetection and other techniques were employed to study tobacco (Nicotiana tabacum) Ndh-defective mutants (DeltandhF). The DeltandhF mutants compared with wild-type plants presented: (i) higher photosystem II : photosystem I (PSII : PSI) ratios; (ii) similar or higher levels of ascorbate, carotenoids, thylakoid peroxidase and superoxide dismutase, yield (Phi(PSII)) and maximal pho…

ChlorophyllChloroplastsTime FactorsLightPhotosystem IIPhysiologyNicotiana tabacumPlant SciencePhotosystem IPhotosynthesisAntioxidantsFluorescenceElectron Transportchemistry.chemical_compoundTobaccoBotanyGene SilencingPhotosynthesisChlorophyll fluorescencePlant ProteinsPhotosystem I Protein ComplexbiologyChlorophyll AReproductionPhotosystem II Protein Complexfood and beveragesNADH Dehydrogenasebiology.organism_classificationChloroplastPhenotypechemistryChlorophyllThylakoidBiophysicsNew Phytologist
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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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Cadmium accumulation and buffering of cadmium-induced stress by arbuscular mycorrhiza in three Pisum sativum L. genotypes

2002

The role of arbuscular mycorrhiza in reducing Cd stress was investigated in three genotypes of Pisum sativum L. (cv. Frisson, VIR4788, VIR7128), grown in soil/sand pot cultures in the presence and absence of 2-3 mg kg(-1) bioavailable Cd, and inoculated or not with the arbuscular mycorrhizal fungus Glomus intraradices. Shoot, root and pod biomass were decreased by Cd in non-mycorrhizal plants. The presence of mycorrhiza attenuated the negative effect of Cd so that shoot biomass and activity of photosystem II, based on chlorophyll a fluorescence, were not significantly different between mycorrhizal plants growing in the presence or absence of the heavy metal (HM). Total P concentrations were…

ChlorophyllGenotypePhysiologyPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein Complexeschemistry.chemical_elementPlant SciencePhosphorus metabolismPisum[SDV.BV.BOT] Life Sciences [q-bio]/Vegetal Biology/BotanicsSativumSymbiosisBotanyPhotosynthesisMycorrhizaSymbiosisComputingMilieux_MISCELLANEOUSAnalysis of VarianceCadmiumbiologyChlorophyll AfungiFungiPeasPhotosystem II Protein Complexfood and beveragesPhosphorus[SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanicsbiology.organism_classificationArbuscular mycorrhizachemistryShootPlant StructuresCadmium
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A battery of toxicity tests as indicators of decontamination in composting oily waste.

2000

Heterogeneous oily waste from an old dumping site was composted in three windrows constructed from different proportions of waste, sewage sludge, and bark. The objectives of this pilot study were to examine the usefulness of composting as a treatment method for this particular waste and to study decontamination in the composting process by using a battery of toxicity tests. Five samples from the windrow having intermediate oil concentrations were tested with toxicity tests based on microbes (Pseudomonas putida growth inhibition test, ToxiChromotest, MetPLATE, and three different modifications of a luminescent bacterial test), enzyme inhibition (reverse electron transport), plants (duckweed …

ChlorophyllHealth Toxicology and MutagenesisPlant DevelopmentGerminationcomplex mixturesWindrowBioremediationPseudomonasEscherichia coliBioassayAnimalsSoil PollutantsDecontaminationSewage sludgeOrganellesPlants MedicinalEnchytraeusbiologyChemistryPublic Health Environmental and Occupational HealthFabaceaeGeneral MedicineHuman decontaminationPlantsbiology.organism_classificationPollutionInvertebratesWaste treatmentPetroleumMetalsEnvironmental chemistryToxicityLuminescent MeasurementsColorimetryDNA DamageEcotoxicology and environmental safety
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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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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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Water-Soluble Chlorophyll Protein (WSCP) Stably Binds Two or Four Chlorophylls

2017

Water-soluble chlorophyll proteins (WSCPs) of class IIa from Brassicaceae form tetrameric complexes containing one chlorophyll (Chl) per apoprotein but no carotenoids. The complexes are remarkably stable toward dissociation and protein denaturation even at 100 °C and extreme pH values, and the Chls are partially protected against photooxidation. There are several hypotheses that explain the biological role of WSCPs, one of them proposing that they function as a scavenger of Chls set free upon plant senescence or pathogen attack. The biochemical properties of WSCP described in this paper are consistent with the protein acting as an efficient and flexible Chl scavenger. At limiting Chl concen…

ChlorophyllModels Molecular0106 biological sciences0301 basic medicineProtein DenaturationHot TemperatureLightLight-Harvesting Protein ComplexesGene ExpressionThylakoids01 natural sciencesBiochemistryProtein Structure SecondaryDissociation (chemistry)law.inventionchemistry.chemical_compoundlawpolycyclic compoundsDenaturation (biochemistry)CarotenoidPlant Proteinschemistry.chemical_classificationSinglet OxygenProtein Stabilityfood and beveragesHydrogen-Ion ConcentrationBiochemistryRecombinant DNAOxidation-ReductionProtein BindingRecombinant Fusion ProteinsBrassicamacromolecular substancesBiology03 medical and health sciencesProtein DomainsTetramerPlant senescenceChlorophyll APeasWaterOxygen030104 developmental biologyWater solubleSolubilitychemistryChlorophyllProtein MultimerizationApoproteins010606 plant biology & botanyBiochemistry
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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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Derivation of coarse-grained simulation models of chlorophyll molecules in lipid bilayers for applications in light harvesting systems

2015

The correct interplay of interactions between protein, pigment and lipid molecules is highly relevant for our understanding of the association behavior of the light harvesting complex (LHCII) of green plants. To cover the relevant time and length scales in this multicomponent system, a multi-scale simulation ansatz is employed that subsequently uses a classical all atomistic (AA) model to derive a suitable coarse grained (CG) model which can be backmapped into the AA resolution, aiming for a seamless conversion between two scales. Such an approach requires a faithful description of not only the protein and lipid components, but also the interaction functions for the indispensable pigment mo…

ChlorophyllModels MolecularChlorophyll bChlorophyll aChlorophyll ABilayerLipid BilayersLight-Harvesting Protein ComplexesGeneral Physics and AstronomyLight-harvesting complexchemistry.chemical_compoundCrystallographychemistryChemical physicsChlorophyllddc:540MoleculeProtein MultimerizationPhysical and Theoretical ChemistryProtein Structure QuaternaryLipid bilayerAnsatz
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