Search results for "STING protein"

showing 10 items of 68 documents

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

Recombinant water-soluble chlorophyll protein from Brassica oleracea var. Botrys binds various chlorophyll derivatives.

2003

A gene coding for water-soluble chlorophyll-binding protein (WSCP) from Brassica oleracea var. Botrys has been used to express the protein, extended by a hexahistidyl tag, in Escherichia coli. The protein has been refolded in vitro to study its pigment binding behavior. Recombinant WSCP was found to bind two chlorophylls (Chls) per tetrameric protein complex but no carotenoids in accordance with previous observations with the native protein [Satoh, H., Nakayama, K., Okada, M. (1998) J. Biol. Chem. 273, 30568-30575]. WSCP binds Chl a, Chl b, bacteriochlorophyll a, and the Zn derivative of Chl a but not pheophytin a, indicating that the central metal ion in Chl is essential for binding. WSCP …

PheophytinChlorophyllProtein FoldingDNA PlantLightTetrameric proteinPhotochemistryPigment bindingPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesProtoporphyrinsmacromolecular substancesBrassicaBiologyBiochemistrychemistry.chemical_compoundPigmentPhytolpolycyclic compoundsChlorophyll bindingChlorophyllidesSinglet OxygenCircular DichroismElectron Spin Resonance Spectroscopyfood and beveragesWaterCarotenoidsRecombinant ProteinsBiochemistrychemistrySolubilitySpectrophotometryChlorophyllvisual_artvisual_art.visual_art_mediumProtein foldingSpin LabelsOxidation-ReductionBiochemistry
researchProduct

Comments on the through space singlet energy transfers and energy migration (exciton) in the light harvesting systems

2008

Recent findings on the photophysical investigations of several cofacial bisporphyrin dyads for through space singlet and triplet energy transfers raised several serious questions about the mechanism of the energy transfers and energy migration in the light harvesting devices, notably LH II, in the heavily studied purple photosynthetic bacteria. The key issue is that for simple cofacial or slipped dyads with controlled geometry using rigid spacers or spacers with limited flexibilities, the fastest possible rates for singlet energy transfer for three examples are in the 10 x 10(9)s(-1) (i.e. just in the 100 ps time scale) for donor-acceptor distances approaching 3.5-3.6 A. The reported time s…

Photosynthetic reaction centreExcitonenergy migrationLight-Harvesting Protein Complexes010402 general chemistryPhotochemistry01 natural sciencesBiochemistryModels BiologicalInorganic ChemistryElectron transferchemistry.chemical_compoundBacterial Proteinslight harvesting systemsSinglet stateBacteriochlorophyllsComputingMilieux_MISCELLANEOUSexcitonenergy transferMolecular Structure010405 organic chemistryChemistrybacteriochlorophyllChromophore0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryRhodopseudomonasChemical physicsPicosecond[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryThermodynamicsPhotosynthetic bacteriaBacteriochlorophyllporphyrin
researchProduct

Direct energy transfer from the major antenna to the photosystem II core complexes in the absence of minor antennae in liposomes

2015

AbstractMinor antennae of photosystem (PS) II, located between the PSII core complex and the major antenna (LHCII), are important components for the structural and functional integrity of PSII supercomplexes. In order to study the functional significance of minor antennae in the energetic coupling between LHCII and the PSII core, characteristics of PSII–LHCII proteoliposomes, with or without minor antennae, were investigated. Two types of PSII preparations containing different antenna compositions were isolated from pea: 1) the PSII preparation composed of the PSII core complex, all of the minor antennae, and a small amount of major antennae (MCC); and 2) the purified PSII dimeric core comp…

Photosynthetic reaction centreLiposomePhotosystem IIChemistryPhotochemistryLight-Harvesting Protein ComplexesBiophysicsPhotosystem II Protein ComplexCell BiologyMinor antennaPhotochemistryFluorescenceBiochemistryProteoliposomePhotosystem IIProtein–protein interactionLight-harvesting complexSpectrometry FluorescenceEnergy TransferThylakoidLiposomesLight-harvesting complexAntenna (radio)PhotosystemBiochimica et Biophysica Acta (BBA) - Bioenergetics
researchProduct

Single amino acids in the lumenal loop domain influence the stability of the major light-harvesting chlorophyll a/b complex.

2004

The major light-harvesting complex of photosystem II (LHCIIb) is one of the most abundant integral membrane proteins. It greatly enhances the efficiency of photosynthesis in green plants by binding a large number of accessory pigments that absorb light energy and conduct it toward the photosynthetic reaction centers. Most of these pigments are associated with the three transmembrane and one amphiphilic alpha helices of the protein. Less is known about the significance of the loop domains connecting the alpha helices for pigment binding. Therefore, we randomly exchanged single amino acids in the lumenal loop domain of the bacterially expressed apoprotein Lhcb1 and then reconstituted the muta…

Photosynthetic reaction centreProtein FoldingPhotosystem IIPigment bindingDNA Mutational AnalysisLight-Harvesting Protein ComplexesPeasPhotosystem II Protein ComplexBiologyBiochemistryTransmembrane proteinProtein Structure SecondaryProtein Structure TertiaryB vitaminsBiochemistryAmino Acid SubstitutionMutant proteinMutagenesis Site-DirectedPoint MutationAmino AcidsIntegral membrane proteinAccessory pigmentGene LibraryPlant ProteinsBiochemistry
researchProduct

Quantum Chemical Simulations of Excited-State Absorption Spectra of Photosynthetic Bacterial Reaction Center and Antenna Complexes

2011

The semiempirical ZINDO/S CIS configuration interaction method has been used to study the ground- and excited-state absorption spectra of wild type and heterodimer M202HL reaction centers from purple bacterium Rhodobacter sphaeroides as well as of peripheral LH2 and LH3 light harvesting complexes from purple bacterium Rhodopseudomonas acidophila. The calculations well reproduce the experimentally observed excited-state absorption spectra between 1000 and 17,000 cm(-1), despite the necessarily limited number of chromophores and protein subunits involved in the calculations. The electron density analysis reveals that the charge transfer between adjacent chromophores dominates the excited-stat…

Photosynthetic reaction centrebiologyAbsorption spectroscopyChemistryLight-Harvesting Protein Complexesbiology.organism_classificationPhotochemistryAbsorptionSurfaces Coatings and FilmsLight-harvesting complexRhodopseudomonasRhodobacter sphaeroidesElectron transferchemistry.chemical_compoundBacterial ProteinsChemical physicsExcited stateMaterials ChemistryQuantum TheoryZINDOBacteriochlorophyllPhysical and Theoretical Chemistryta116The Journal of Physical Chemistry B
researchProduct

Acceleration of the through space S1 energy transfer rates in cofacial bisporphyrin bio-inspired models by virtue of substituents effect on the Först…

2011

The singlet k(ET) for cofacial β-octaalkylporphyrin/bis(meso-aryl)porphyrin dyads increases linearly with the gap between the donor-acceptor 0-0 fluorescence peaks at 77 K.

PorphyrinsEnergy transferLight-Harvesting Protein ComplexesMetals and AlloysAntenna effectGeneral ChemistrySpace (mathematics)PorphyrinFluorescenceCatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialschemistry.chemical_compoundAccelerationSpectrometry FluorescenceBacterial ProteinsEnergy TransferModels ChemicalchemistryChemical physicsMaterials ChemistryCeramics and CompositesSinglet stateAtomic physicsPhotosystemChemical Communications
researchProduct

Refolding of the integral membrane protein light-harvesting complex II monitored by pulse EPR

2009

The major light-harvesting chlorophyll a / b complex (LHCII) of the photosynthetic apparatus in plants self-organizes in vitro. The recombinant apoprotein, denatured in dodecyl sulfate, spontaneously folds when it is mixed with its pigments, chlorophylls, and carotenoids in detergent solution, and assembles into structurally authentic LHCII in the course of several minutes. Pulse EPR techniques, specifically double-electron-electron resonance (DEER), have been used to analyze protein folding during this process. Pairs of nitroxide labels were introduced site-specifically into recombinant LHCII and shown not to affect the stability and function of the pigment-protein complex. Interspin dist…

Protein DenaturationProtein FoldingTime FactorsMultidisciplinaryPulsed EPRSuperhelixChemistryElectron Spin Resonance SpectroscopyLight-Harvesting Protein ComplexesPeasMembrane ProteinsElectronsBiological SciencesModels BiologicalProtein Structure SecondaryTransmembrane domainB vitaminsCrystallographyProtein structureMutationHelixSpin LabelsProtein foldingApoproteinsIntegral membrane proteinProceedings of the National Academy of Sciences
researchProduct

Identification of N- and C-terminal Amino Acids of Lhca1 and Lhca4 Required for Formation of the Heterodimeric Peripheral Photosystem I Antenna LHCI-…

2002

Apoproteins of higher plant light-harvesting complexes (LHC) share considerable amino acid sequence identity/similarity. Despite this fact, they occur in different oligomeric states (i.e., monomeric, dimeric, and trimeric). As a step toward understanding the underlying structure requirements for different oligomerization behavior, we analyzed whether amino acids at the N- and C-termini of Lhca1 and Lhca4 are involved in the formation of the heterodimeric LHCI-730. Using altered proteins produced by deletion or site-directed mutagenesis for reconstitution, we were able to identify amino acids required for the assembly of LHCI-730. At the N-terminus of Lhca1, W4 is involved in heterodimerizat…

StereochemistryDimerPhotosynthetic Reaction Center Complex ProteinsMutantLight-Harvesting Protein ComplexesBiologyPhotosystem IBiochemistrychemistry.chemical_compoundResidue (chemistry)Point MutationAmino AcidsPeptide sequencePlant ProteinsSequence Deletionchemistry.chemical_classificationPhotosystem I Protein ComplexArabidopsis ProteinsMutagenesisRecombinant ProteinsAmino acidMonomerBiochemistrychemistryChlorophyll Binding ProteinsDimerizationBiochemistry
researchProduct

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
researchProduct