Search results for "Photos"

showing 10 items of 701 documents

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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Chlorophyll a fluorescence, antioxidant enzymes and lipid peroxidation in tomato in response to ozone and benomyl

2001

Ozone is a widely distributed phytotoxic air pollutant and is known to reduce the yield of several important agricultural crops in Spain. However, benomyl has been found to lessen the adverse impact of ozone on plants. We studied the effects of ozone and benomyl on chlorophyll a fluorescence, antioxidant enzymes, and lipid peroxidation in tomato (Lycopersicon esculentum Mill. cv. Tiny Tim) grown in open-top chambers in the field. Our results indicate that benomyl prevented the peroxidation of membrane lipids and increased protection of PSII from ozone. There was also a significant reduction in the activity of the antioxidant enzyme superoxide dismutase in ozone-exposed plants that had not b…

ChlorophyllOzoneAntioxidantHealth Toxicology and Mutagenesismedicine.medical_treatmentToxicologyPhotosynthesisFluorescenceSuperoxide dismutaseLipid peroxidationchemistry.chemical_compoundOzoneSolanum lycopersicumBotanymedicineChlorophyll fluorescenceAir PollutantsbiologySuperoxide DismutaseChemistryChlorophyll Afungifood and beveragesBenomylGeneral Medicinebiology.organism_classificationPollutionFungicides IndustrialPlant LeavesOxidative StressHorticultureAir Pollution Indoorbiology.proteinBenomylLipid PeroxidationSolanaceaeEnvironmental Pollution
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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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Characterization of the Fast and Slow Reversible Components of Non-Photochemical Quenching in Isolated Pea Thylakoids by Picosecond Time-Resolved Chl…

1999

The fast and slow reversible components of non-photochemical chlorophyll fluorescence quenching commonly assigned to the qE and the qI mechanism have been studied in isolated pea thylakoids which were prepared from leaves after a moderate photoinhibitory treatment. Chlorophyll fluorescence decays were measured at picosecond resolution and analyzed on the basis of the heterogeneous exciton/radical pair equilibrium model. Our results show that the fast reversible non-photochemical quenching is completely assigned to the PS II antenna and is related to zeaxanthin. The slow reversible qI type quenching is located at the PS II reaction center and involves enhanced nonradiative decay of the prima…

ChlorophyllPhotosynthetic reaction centrePhotoinhibitionQuenching (fluorescence)ChemistryNon-photochemical quenchingPeasPhotochemistryBiochemistryKineticsSpectrometry FluorescencePicosecondExcited stateThylakoidChlorophyll fluorescencePlant ProteinsBiochemistry
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Assessing and modeling nitrite inhibition in microalgae-bacteria consortia for wastewater treatment by means of photo-respirometric and chlorophyll f…

2022

Abstract Total nitrite (TNO2 = HNO2 + NO−2) accumulation due to the activity of ammonia-oxidizing bacteria (AOB) was monitored in microalgae-bacteria consortia, and the inhibitory effect of nitrite/free nitrous acid (NO2-N/FNA) on microalgae photosynthesis and inhibition mechanism was studied. A culture of Scenedesmus was used to run two sets of batch reactors at different pH and TNO2 concentrations to evaluate the toxic potential of NO2-N and FNA. Photo-respirometric tests showed that NO2-N accumulation has a negative impact on net oxygen production rate (OPRNET). Chlorophyll a fluorescence analysis was used to examine the biochemical effects of NO2-N stress and the mechanism of NO2-N inhi…

ChlorophyllPhotosynthetic reaction centrechemistry.chemical_classificationNitrous acidChlorophyll aEnvironmental EngineeringBacteriabiologyChemistryChlorophyll AElectron acceptorbiology.organism_classificationPollutionFluorescenceWater Purificationchemistry.chemical_compoundMicroalgaeEnvironmental ChemistryNitriteWaste Management and DisposalChlorophyll fluorescenceNitritesScenedesmusPhotosystemNuclear chemistryScience of The Total Environment
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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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