Search results for " reaction center"

showing 3 items of 33 documents

De-epoxidation of Violaxanthin after Reconstitution into Different Carotenoid Binding Sites of Light-harvesting Complex II

2001

In higher plants, the de-epoxidation of violaxanthin (Vx) to antheraxanthin and zeaxanthin is required for the pH-dependent dissipation of excess light energy as heat and by that process plays an important role in the protection against photo-oxidative damage. The de-epoxidation reaction was investigated in an in vitro system using reconstituted light-harvesting complex II (LHCII) and a thylakoid raw extract enriched in the enzyme Vx de-epoxidase. Reconstitution of LHCII with varying carotenoids was performed to replace lutein and/or neoxanthin, which are bound to the native complex, by Vx. Recombinant LHCII containing either 2 lutein and 1 Vx or 1.6 Vx and 1.1 neoxanthin or 2.8 Vx per mono…

chemistry.chemical_classificationLuteinBinding SitesAntheraxanthinPhotosynthetic Reaction Center Complex Proteinsfood and beveragesCell BiologyXanthophyllsbeta CaroteneBiochemistryZeaxanthinKineticschemistry.chemical_compoundchemistryNeoxanthinBiochemistryThylakoidXanthophyllBiophysicsEpoxy CompoundsMolecular BiologyCarotenoidViolaxanthinJournal 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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Protein-Matrix Coupling/Uncoupling in “Dry” Systems of Photosynthetic Reaction Centre Embedded in Trehalose/Sucrose: The Origin of Trehalose Peculiar…

2008

trehalose reaction center
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