Search results for "Light harvesting complex I"

showing 5 items of 5 documents

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
researchProduct

Crystallization of Light-Harvesting Complex II From Vicia Faba (Fabaceae)

1998

The most abundant chlorophyll binding complex in plants is the intrinsic light-harvesting complex II (LHC II), comprising about half of the total chlorophyll in thylakoid membranes. The structure of LHC II has been determined by electron crystallography, providing a three-dimensional map at 3.4 A (1). Nevertheless, high-resolution structure based on x-ray crystallography is still missing because of the lack of highly ordered 3-D crystals. While delipidation of membrane proteins suitable for high-quality 3-D crystals seems to be a prerequisite, in case of LHC H delipidation leads to a loss of the ability to crystallize. So far, standard purification methods like chromatography have been proo…

Electron crystallographyChemistryFabaceaelaw.inventionVicia fabachemistry.chemical_compoundCrystallographylawChlorophyllThylakoidBotanyChlorophyll bindingCrystallizationLight harvesting complex II
researchProduct

Lhca5 interaction with plant photosystem I

2006

AbstractIn the outer antenna (LHCI) of higher plant photosystem I (PSI) four abundantly expressed light-harvesting protein of photosystem I (Lhca)-type proteins are organized in two heterodimeric domains (Lhca1/Lhca4 and Lhca2/Lhca3). Our cross-linking studies on PSI-LHCI preparations from wildtype Arabidopsis and pea plants indicate an exclusive interaction of the rarely expressed Lhca5 light-harvesting protein with LHCI in the Lhca2/Lhca3-site. In PSI particles with an altered LHCI composition Lhca5 assembles in the Lhca1/Lhca4 site, partly as a homodimer. This flexibility indicates a binding-competitive model for the LHCI assembly in plants regulated by molecular interactions of the Lhca…

Models MolecularPhotosystem IArabidopsisLight-Harvesting Protein ComplexesBiophysicsPhotosystem IBiochemistrychemistry.chemical_compoundLight harvesting complex IStructural BiologyArabidopsisGeneticsMolecular BiologyLhca5Molecular interactionsPhotosystem I Protein ComplexbiologyArabidopsis ProteinsPeasWild typefood and beveragesArabidopsis ProteinsCell BiologyLight-Harvesting Protein Complexesbiology.organism_classificationCrystallographychemistryChlorophyllBiophysicsLight-harvesting complex ICross-linkingFEBS Letters
researchProduct

Site-specific incorporation of perylene into an N-terminally modified light-harvesting complex II.

2010

Employing the utility of the native chemical ligation, site-specific attachment of an ultrastable perylene dye to a derivative of the major light-harvesting complex (LHCII) was demonstrated. Biochemical analysis of the conjugate indicated that the structure and function of LHCII remain largely unaffected by the N-terminal modification.

Molecular Sequence DataLight-Harvesting Protein Complexes010402 general chemistryPhotochemistry01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundPhysical and Theoretical ChemistryFLUORESCENCEPROTEIN LIGATIONPerylene030304 developmental biologyFluorescent DyesPlant Proteins0303 health sciencesSTABILITYOrganic ChemistryMICROSCOPYPlantsNative chemical ligationFluorescenceLIVE CELLS0104 chemical sciencesStructure and functionchemistryBiophysicsSMALL-MOLECULE PROBESCYSTEINEPeryleneDerivative (chemistry)DYESCysteineConjugateLight harvesting complex IIOrganicbiomolecular chemistry
researchProduct

Assemblies of semiconductor quantum dots and light-harvesting-complex II

2010

Abstract A novel hybrid system composed of fluorescent core/shell semiconductor quantum dots and the light harvesting complex II (LHCIIb), a membrane protein of higher plants, has been assembled. Experiments with different mutants show that hybrid formation can be mediated by a C-terminal His 6 tag attached to the protein as well as by positive charges of the first N-terminal amino acids of LHCIIb. Quenching of the quantum dot fluorescence upon binding of LHCIIb was partially attributed to energy transfer from the quantum dots to LHCIIb.

Quenching (fluorescence)ChemistryEnergy transfertechnology industry and agricultureBiophysicsNanotechnologyGeneral Chemistryequipment and suppliesCondensed Matter PhysicsBiochemistryFluorescenceAtomic and Molecular Physics and OpticsLight-harvesting complexSemiconductor quantum dotsQuantum dotChemical physicsHybrid materialLight harvesting complex IIJournal of Luminescence
researchProduct