Search results for "Light-harvesting"

showing 10 items of 93 documents

Pigment organization and energy transfer dynamics in isolated photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, P…

2002

Abstract Green plant photosystem I (PSI) consists of at least 18 different protein subunits. The roles of some of these protein subunits are not well known, in particular those that do not occur in the well characterized PSI complexes from cyanobacteria. We investigated the spectroscopic properties and excited-state dynamics of isolated PSI-200 particles from wild-type and mutant Arabidopsis thaliana plants devoid of the PSI-G, PSI-K, PSI-L, or PSI-N subunit. Pigment analysis and a comparison of the 5K absorption spectra of the various particles suggests that the PSI-L and PSI-H subunits together bind approximately five chlorophyll a molecules with absorption maxima near 688 and 667nm, that…

Time FactorsAbsorption spectroscopyProtein subunitPhotosynthetic Reaction Center Complex ProteinsArabidopsisLight-Harvesting Protein ComplexesBiophysicsBiologyPhotosystem Ichemistry.chemical_compoundPhase (matter)MoleculePlant ProteinsQuantitative Biology::BiomoleculesPhotosystem I Protein ComplexTemperaturePigments Biologicalbeta CaroteneFluorescenceKineticsCrystallographySpectrometry FluorescenceEnergy TransferchemistryChlorophyllThermodynamicsHigh Energy Physics::ExperimentAbsorption (chemistry)Research Article
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Excited State Dynamics in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower Investigated by Transient Fluorescence Spectroscopy

2008

The present study describes the fluorescence emission properties of recombinant water-soluble chlorophyll (Chl) protein (WSCP) complexes reconstituted with either Chl a or Chl b alone (Chl a only or Chl b only WSCP, respectively) or mixtures of both pigments at different stoichiometrical ratios. Detailed investigations were performed with time and space correlated ps fluorescence spectroscopy within the temperature range from 10 to 295 K. The following points were found: (a) The emission spectra at room temperature (295 K) are well characterized by bands with a dominating Lorentzian profile broadened due to phonon scattering and peak positions located at 677, 684 and 693 nm in the case of C…

Time FactorsLight-Harvesting Protein ComplexesTemperatureAnalytical chemistryWaterBrassicaAtmospheric temperature rangeFluorescenceRecombinant ProteinsSpectral lineFluorescence spectroscopySurfaces Coatings and FilmsPigmentchemistry.chemical_compoundSpectrometry FluorescenceSolubilitychemistryvisual_artExcited stateChlorophyllMaterials Chemistryvisual_art.visual_art_mediumEmission spectrumPhysical and Theoretical ChemistryPlant ProteinsThe Journal of Physical Chemistry B
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Ultrafast excitation dynamics of low energy pigments in reconstituted peripheral light-harvesting complexes of photosystem I

2000

AbstractUltrafast dynamics of a reconstituted Lhca4 subunit from the peripheral LHCI-730 antenna of photosystem I of higher plants were probed by femtosecond absorption spectroscopy at 77 K. Intramonomeric energy transfer from chlorophyll (Chl) b to Chl a and energy equilibration between Chl a molecules observed on the subpicosecond time scale are largely similar to subpicosecond energy equilibration processes within LHCII monomers. However, a 5 ps equilibration process in Lhca4 involves unique low energy Chls in LHCI absorbing at 705 nm. These pigments localize the excitation both in the Lhca4 subunit and in LHCI-730 heterodimers. An additional 30–50 ps equilibration process involving red …

Time-resolved spectroscopyPhotosystem I0106 biological sciencesAbsorption spectroscopyPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsPhotochemistryPhotosystem I01 natural sciences7. Clean energyBiochemistryFluorescence spectroscopyLight-harvesting complexExcitation energy transfer03 medical and health scienceschemistry.chemical_compoundStructural BiologyUltrafast laser spectroscopyGeneticsMolecular BiologyPlant Proteins030304 developmental biology0303 health sciencesPhotosystem I Protein ComplexSpectrophotometry AtomicPigments BiologicalCell BiologyPlantsLHCI-730 heterodimerEnergy TransferchemistryAntennaChlorophyllPicosecondChlorophyll Binding ProteinsLight-harvesting complexTime-resolved spectroscopyDimerization010606 plant biology & botanyFEBS Letters
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Refined carotenoid analysis of the major light-harvesting complex of Mantoniella squamata

1997

The major light-harvesting complex (LHC) of the prasinophycean alga Mantoniella squamata is unique compared to other chlorophyll (Chl) a/b-binding LHC with respect to the primary protein structure and the pigmentation. Although the presence of Chl a, Chl b, a Chl c-type pigment and the xanthophylls neoxanthin, violaxanthin and prasinoxanthin was clearly determined, several carotenoids remained unidentified or were described controversially. We re-analysed the carotenoid composition and identified a new set of xanthophylls present in the LHC: uriolide, micromonol, micromonal and dihydrolutein. Additionally, one hydrophobic component was detected, presumably a xanthophyll. The pigment analysi…

chemistry.chemical_classificationChlorophyll aChromatographyPhysiologyfood and beveragesmacromolecular substancesPlant ScienceBiologyLight-harvesting complexchemistry.chemical_compoundPigmentchemistryBiochemistryNeoxanthinXanthophyllChlorophyllvisual_artpolycyclic compoundsvisual_art.visual_art_mediumCarotenoidViolaxanthinPhotosynthetica
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Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata.

1994

The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.

chemistry.chemical_classificationChlorophyll abiologyBinding proteinProtein primary structureCell BiologyPlant ScienceGeneral Medicinebiology.organism_classificationBiochemistryMolecular biologyAmino acidLight-harvesting complexchemistry.chemical_compoundProtein sequencingBiochemistrychemistryMantoniellaPeptide sequencePhotosynthesis research
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Pigment-pigment interactions and secondary structure of reconstituted algal chlorophyll a/b-binding light-harvesting complexes of Chlorella fusca wit…

1995

Earlier we have shown by in vitro reconstitution experiments that the pigment composition of the chlorophyll alb-binding light-harvesting complex of the green alga Chlorella fusca could be altered in a relatively broad range (Meyer and Wilhelm 1993). In this study we used these reconstituted complexes of different pigment loading to analyze the excitonic interactions between the pigment molecules and the secondary structure by means of circular dichroism spectra in the visible and the far UV spectral regions, respectively. We found that, in contrast to the expectations, the pigment composition and pigment content hardly affected the circular dichroism spectra in the visible spectral region.…

chemistry.chemical_classificationChlorophyll bChlorophyll aCircular dichroismCell BiologyPlant ScienceGeneral MedicineBiologyPhotochemistryBiochemistryLight-harvesting complexchemistry.chemical_compoundPigmentchemistryvisual_artChlorophyllXanthophyllvisual_art.visual_art_mediumsense organsProtein secondary structurePhotosynthesis Research
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The Binding of Xanthophylls to the Bulk Light-harvesting Complex of Photosystem II of Higher Plants

2002

The pigment composition of the light-harvesting complexes (LHCs) of higher plants is highly conserved. The bulk complex (LHCIIb) binds three xanthophyll molecules in combination with chlorophyll (Chl) a and b. The structural requirements for binding xanthophylls to LHCIIb have been examined using an in vitro reconstitution procedure. Reassembly of the monomeric recombinant LHCIIb was performed using a wide range of native and nonnative xanthophylls, and a specific requirement for the presence of a hydroxy group at C-3 on a single β-end group was identified. The presence of additional substituents (e.g.at C-4) did not interfere with xanthophyll binding, but they could not, on their own, supp…

chemistry.chemical_classificationLuteinPhotosystem IIfood and beveragesCell BiologyBiologyXanthophyll bindingBiochemistryeye diseasesZeaxanthinLight-harvesting complexchemistry.chemical_compoundchemistryBiochemistryXanthophyllMolecular BiologyCarotenoidViolaxanthinJournal of Biological Chemistry
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Ligand requirement for LHC I reconstitution

1998

Knowledge of the structure of photosynthetic light harvesting complexes is essential for understanding their function. Reconstitution of light harvesting complexes proved to be a very powerful tool for such structure analyses. In this way evidence was obtained for the central role of lutein and chlorophylls for LHCII structure (1) which was later confirmed by electron crystallographic analyses (2). Employing mutated, bacterial overexpressed LHCII apoproteins, amino acids could be identified which are involved in trimerization of LHCII and probably in binding of phosphatidylglycerol (3).

chemistry.chemical_classificationPhosphatidylglycerolLight-harvesting complexchemistry.chemical_compoundLuteinchemistryBiophysicsPhotosynthesisPhotosystem ILigand (biochemistry)Function (biology)Amino acid
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Pigment ligation to proteins of the photosynthetic apparatus in higher plants

1997

Ligation of pigments to proteins of the thylakoid membrane is a central step in the assembly of the photosynthetic apparatus in higher plants. Because of the potentially damaging photooxidative activity of chlorophylls, it is likely that between their biosynthesis and final assembly, chlorophylls will always be bound to protein complexes in which photooxidation is prevented by quenchers such as carotenoids. Such complexes may include chlorophyll carriers and/or membrane receptors involved in protein insertion into the membrane. Many if not all pigment-protein complexes of the thylakoid are stabilised towards protease attack by bound pigments. The major light-harvesting chlorophyll a/b prote…

chemistry.chemical_classificationPhysiologyfood and beveragesLight-harvesting complexes of green plantsCell BiologyPlant ScienceGeneral MedicineBiologyPhotosynthesisLight-harvesting complexchemistry.chemical_compoundchemistryBiochemistryThylakoidChlorophyllXanthophyllGeneticsProtein foldingCarotenoidPhysiologia Plantarum
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Carotenoids and the Assembly of Light-harvesting Complexes

2006

Carotenoids are constitutive components of all light-harvesting complexes in plants and many such complexes in bacteria. In the crystal structures of several light-harvesting complexes, carotenoids are seen to span the lipid bilayer and connect components of the complex on both membrane surfaces and/or to mediate the interaction of transmembrane protein helices. This important stabilizing function suggests that these pigments are also actively involved in the assembly of light-harvesting complexes. Verification of this notion appears too ambitious a goal at present, as the question of how the pigment-protein complexes of the photosynthetic apparatus are assembled is still open. However, inf…

chemistry.chemical_classificationbiologyChemistryorganic chemicalsfood and beveragesmacromolecular substancesbiology.organism_classificationPhotosynthesisbiological factorsTransmembrane proteinLight-harvesting complexRhodobacter sphaeroidesBiochemistrypolycyclic compoundsLipid bilayerCarotenoidBiogenesisFunction (biology)
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