Search results for "Photosystem I"

showing 6 items of 86 documents

Pigment composition of PS II pigment protein complexes purified by anion exchange chromatography. identification of xanthophyll cycle pigment binding…

1997

Summary The pigment composition of the chlorophyll binding proteins of Photosystem II (PS II) of spinach ( Spinacea oleracea L.) has been determined using sucrose gradient ultracentrifugation, anion exchange chromatography and HPLC based pigment analysis. The xanthophyll cycle pigments violaxanthin, antheraxanthin and zeaxanthin were exclusively found in the proteins of the outer PS II antenna, with the highest amounts being present in the minor chlorophyll alb binding proteins CP 29 and CP 26. PS II core particles containing the reaction centre proteins D1, D2, cytochrome b 559 and the proteins of the inner antenna CP 47 and CP 43 bind β-carotene as the only carotenoid. The presence of the…

chemistry.chemical_classificationChromatographyPhotosystem IIPhysiologyAntheraxanthinPigment bindingPlant ScienceZeaxanthinchemistry.chemical_compoundBiochemistrychemistryXanthophyllChlorophyll bindingsense organsChlorophyll Binding ProteinsAgronomy and Crop ScienceViolaxanthinJournal of Plant Physiology
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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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Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR

2015

The major light harvesting complex II (LHCII) of green plants plays a key role in the absorption of sunlight, the regulation of photosynthesis, and in preventing photodamage by excess light. The latter two functions are thought to involve the lumenal loop and the N-terminal domain. Their structure and mobility in an aqueous environment are only partially known. Electron paramagnetic resonance (EPR) has been used to measure the structure of these hydrophilic protein domains in detergent-solubilized LHCII. A new technique is introduced to prepare LHCII trimers in which only one monomer is spin-labeled. These heterogeneous trimers allow to measure intra-molecular distances within one LHCII mon…

inorganic chemicalsModels MolecularProtein ConformationProtein domainTrimerContext (language use)complex mixturesBiochemistrylaw.inventionchemistry.chemical_compoundBiopolymersProtein structurelawElectron paramagnetic resonanceMolecular BiologySuperhelixfungiElectron Spin Resonance SpectroscopyPhotosystem II Protein ComplexCell Biologyequipment and suppliesCrystallographyMonomerModels ChemicalchemistryThylakoidProtein Structure and FoldingbacteriaJournal of Biological Chemistry
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Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes

1998

AbstractPrevious studies directed towards understanding phosphorylation of the chlorophyll a/b binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhcb1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of wh…

inorganic chemicalsPhotosystem IIMacromolecular SubstancesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsmacromolecular substancesBiologyBiochemistryDNA-binding proteinProtein kinaseThylakoid membraneSubstrate Specificitylaw.inventionStructural BiologylawGeneticsProtein phosphorylationAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyPlant ProteinsKinasePeasPeaPhotosystem II Protein Complexfood and beveragesCell BiologySpinachPeptide FragmentsRecombinant Proteinsenzymes and coenzymes (carbohydrates)BiochemistryThylakoidRecombinant DNALight harvesting proteinPhosphorylationbacteriaCarrier ProteinsProtein KinasesFEBS Letters
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KOSMOS 2017 Peru Side Experiment: nutrients, phytoplankton abundances, enzyme rates, photophysiology

2022

This data was collected during an short-term incubation experiment in March 2017 that investigated the response of a surface plankton community to upwelling. This experiment was carried in the framework of the SFB754-funded KOSMOS mesocosm study that took place in La Punta, Callao, Peru between February-April 2017. A total of six different treatments were used to disentangle chemical and biological characteristics of deep water that influence surface plankton blooms: 2 different deep water sources with different nutrient concentrations; 3 treatments to distinguish the effects of inorganic nutrients, organic nutrients and deep water microbial populations. Measured variables include inorganic…

ratioDay of experimentSFB754colored dissolved organic matter at 325 nmNitriteChlorophyll aAbsorption coefficient colored dissolved organic matter at 254 nmClimate - Biogeochemistry Interactions in the Tropical Ocean (SFB754)colorimetric determinationFluorometerFluorometricNitrateNanoplanktonPhytoplankton cells phycocyanin-containing (FL-4)PicoeukaryotesFluorometer fast repetition rateCalculatedFlow cytometryNutrient consumption ratioforward scatterSynechococcusupwelling systemsMesocosm experimentSpectrophotometricClimate Biogeochemistry Interactions in the Tropical Ocean SFB754SilicateBiogeochemistryBiospheric SciencesMaximum photochemical quantum yield of photosystem IIenzyme activitycell sizeDissolved inorganic nitrogen/dissolved inorganic phosphorus ratioKOSMOS_2017chainsAbsorption coefficient colored dissolved organic matter 250 nm/365 nm ratioeastern tropical South Pacific OceanKOSMOSExcess phosphateAbsorption coefficient colored dissolved organic matter at 325 nmNatural SciencesGeosciencescolored dissolved organic matter at 254 nmphycocyanin containing FL 4Absorption coefficientPhosphateTank numberPhytoplankton cells chainsNetwork of Leading European AQUAtic MesoCOSM Facilities Connecting Mountains to Oceans from the ArctReplicatenutrientsfast repetition rateDATE TIMECryptophytesMicrophytoplanktonPhytoplankton cellsLeucine aminopeptidase activityDissolved inorganic nitrogen dissolved inorganic phosphorus ratiofungiEnzymatic assayContinuous flow analyserTreatmentDATE/TIMEcolored dissolved organic matter 250 nm 365 nmPhytoplanktonPhytoplankton cell size forward scatterNetwork of Leading European AQUAtic MesoCOSM Facilities Connecting Mountains to Oceans from the Arctic to the Mediterranean (AQUACOSM)CDOMContinuous flow analyser colorimetric determinationNitrate and Nitrite
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