Search results for "Photosystem I Protein Complex"

showing 10 items of 16 documents

Chlorophyll fluorescence emission spectrum inside a leaf

2008

International audience; Chlorophyll a fluorescence can be used as an early stress indicator. Fluorescence is also connected to photosynthesis so it can be proposed for global monitoring of vegetation status from a satellite platform. Nevertheless, the correct interpretation of fluorescence requires accurate physical models. The spectral shape of the leaf fluorescence free of any re-absorption effect plays a key role in the models and is difficult to measure. We present a vegetation fluorescence emission spectrum free of re-absorption based on a combination of measurements and modelling. The suggested spectrum takes into account the photosystem I and II spectra and their relative contributio…

0106 biological sciencesChlorophyllChlorophyll aSpectral shape analysisI REACTION CENTERSSPINACH THYLAKOID MEMBRANES[SDU.ASTR.EP]Sciences of the Universe [physics]/Astrophysics [astro-ph]/Earth and Planetary Astrophysics [astro-ph.EP]PHOTOSYNTHETIC MEMBRANEPhotosystem I01 natural sciencesSpectral lineHIGHER-PLANTSPROTEIN COMPLEXES03 medical and health scienceschemistry.chemical_compoundmedicineEmission spectrumPhysical and Theoretical ChemistryChlorophyll fluorescenceLIGHT-HARVESTING COMPLEX030304 developmental biologyRemote sensing0303 health sciencesPhotosystem I Protein Complex[SDU.ASTR]Sciences of the Universe [physics]/Astrophysics [astro-ph]Photosystem II Protein Complexfood and beveragesFluorescencePlant LeavesSpectrometry FluorescenceROOM-TEMPERATUREchemistryPHOTOSYSTEM-I[SDU]Sciences of the Universe [physics]Espectroscòpia de fluorescènciaARABIDOPSIS-THALIANAmedicine.symptomVegetation (pathology)ENERGY-TRANSFER010606 plant biology & botany
researchProduct

Functional rearrangement of the light-harvesting antenna upon state transitions in a green alga

2014

AbstractState transitions in the green alga Chlamydomonas reinhardtii serve to balance excitation energy transfer to photosystem I (PSI) and to photosystem II (PSII) and possibly play a role as a photoprotective mechanism. Thus, light-harvesting complex II (LHCII) can switch between the photosystems consequently transferring more excitation energy to PSII (state 1) or to PSI (state 2) or can end up in LHCII-only domains. In this study, low-temperature (77 K) steady-state and time-resolved fluorescence measured on intact cells of Chlamydomonas reinhardtii shows that independently of the state excitation energy transfer from LHCII to PSI or to PSII occurs on two main timescales of <15 ps and …

0106 biological sciencesPhotosystem IIEnergy transferBiophysicsLight-Harvesting Protein ComplexesphotosystemChlamydomonas reinhardtiiPhotosystem IPhotochemistry01 natural sciences03 medical and health sciencesstate transitionsgreen algaSDG 7 - Affordable and Clean Energy030304 developmental biologyPhotosystem0303 health sciencesenergy transfer/dk/atira/pure/sustainabledevelopmentgoals/affordable_and_clean_energybiologyPhotosystem I Protein ComplexChemistryta1182Photosystem II Protein ComplexState (functional analysis)biology.organism_classificationFluorescenceCell BiophysicsAtomic physicsExcitationChlamydomonas reinhardtii010606 plant biology & botanyBiophysical journal
researchProduct

Chlorophyll b is involved in long-wavelength spectral properties of light-harvesting complexes LHC I and LHC II.

2001

AbstractChlorophyll (Chl) molecules attached to plant light-harvesting complexes (LHC) differ in their spectral behavior. While most Chl a and Chl b molecules give rise to absorption bands between 645 nm and 670 nm, some special Chls absorb at wavelengths longer than 700 nm. Among the Chl a/b-antennae of higher plants these are found exclusively in LHC I. In order to assign this special spectral property to one chlorophyll species we reconstituted LHC of both photosystem I (Lhca4) and photosystem II (Lhcb1) with carotenoids and only Chl a or Chl b and analyzed the effect on pigment binding, absorption and fluorescence properties. In both LHCs the Chl-binding sites of the omitted Chl species…

Chlorophyll bChlorophyllPhotosystem IIPigment bindingPhotosynthetic Reaction Center Complex ProteinsBiophysicsLight-Harvesting Protein ComplexesPhotosystem IPhotochemistryBiochemistryAbsorptionLight-harvesting complexReconstitutionchemistry.chemical_compoundSolanum lycopersicumStructural BiologySpinacia oleraceaGeneticsChlorophyll bindingCentrifugation Density GradientMolecular BiologyChlorophyll fluorescenceLong-wavelength chlorophyllBinding SitesPhotosystem I Protein ComplexChemistryChlorophyll ATemperaturePhotosystem II Protein ComplexLight-harvesting complexes of green plantsCell BiologyPigments BiologicalPlant LeavesSpectrometry FluorescenceLight-harvesting complexChlorophyll fluorescenceChlorophyll bindingProtein BindingFEBS letters
researchProduct

Pigment binding of photosystem I light-harvesting proteins.

2002

Light-harvesting complexes (LHC) of higher plants are composed of at least 10 different proteins. Despite their pronounced amino acid sequence homology, the LHC of photosystem II show differences in pigment binding that are interpreted in terms of partly different functions. By contrast, there is only scarce knowledge about the pigment composition of LHC of photosystem I, and consequently no concept of potentially different functions of the various LHCI exists. For better insight into this issue, we isolated native LHCI-730 and LHCI-680. Pigment analyses revealed that LHCI-730 binds more chlorophyll and violaxanthin than LHCI-680. For the first time all LHCI complexes are now available in t…

ChlorophyllChlorophyll aPhotosystem IIPigment bindingPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyXanthophyllsPhotosystem IBiochemistrychemistry.chemical_compoundPigmentSolanum lycopersicumMolecular BiologyP700Binding SitesPhotosystem I Protein ComplexChlorophyll Afood and beveragesPhotosystem II Protein ComplexCell BiologyPigments Biologicalbeta CarotenePlant LeavesSpectrometry FluorescencechemistryBiochemistryChlorophyllvisual_artvisual_art.visual_art_mediumViolaxanthinThe Journal of biological chemistry
researchProduct

Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

2005

A new potential light-harvesting protein, named Lhca5, was recently detected in higher plants. Because of the low amount of Lhca5 in thylakoid membranes, the isolation of a native Lhca5 pigment-protein complex has not been achieved to date. Therefore, we used in vitro reconstitution to analyze whether Lhca5 binds pigments and is actually an additional light-harvesting protein. By this approach we could demonstrate that Lhca5 binds pigments in a unique stoichiometry. Analyses of pigment requirements for light-harvesting complex formation by Lhca5 revealed that chlorophyll b is the only indispensable pigment. Fluorescence measurements showed that ligated chlorophylls and carotenoids are arran…

ChlorophyllChlorophyll bPigment bindingArabidopsisLight-Harvesting Protein Complexesmacromolecular substancesBiologyPhotosystem IBiochemistryFluorescencechemistry.chemical_compoundProtein structureProtein Structure QuaternaryMolecular BiologyPhotosystemPhotosystem I Protein ComplexArabidopsis ProteinsPigments BiologicalCell BiologyCarotenoidsFluorescenceBiochemistrychemistryThylakoidChlorophyll Binding ProteinsChlorophyll Binding ProteinsDimerizationJournal of Biological Chemistry
researchProduct

Inactivation of a plastid evolutionary conserved gene affects PSII electron transport, life span and fitness of tobacco plants

2007

Chloroplasts contain a plastoquinone-NADH-oxidoreductase (Ndh) complex involved in protection against stress and the maintenance of cyclic electron flow. Inactivation of the Ndh complex delays the development of leaf senescence symptoms. Chlorophyll a fluorescence measurements, blue native gel electrophoresis, immunodetection and other techniques were employed to study tobacco (Nicotiana tabacum) Ndh-defective mutants (DeltandhF). The DeltandhF mutants compared with wild-type plants presented: (i) higher photosystem II : photosystem I (PSII : PSI) ratios; (ii) similar or higher levels of ascorbate, carotenoids, thylakoid peroxidase and superoxide dismutase, yield (Phi(PSII)) and maximal pho…

ChlorophyllChloroplastsTime FactorsLightPhotosystem IIPhysiologyNicotiana tabacumPlant SciencePhotosystem IPhotosynthesisAntioxidantsFluorescenceElectron Transportchemistry.chemical_compoundTobaccoBotanyGene SilencingPhotosynthesisChlorophyll fluorescencePlant ProteinsPhotosystem I Protein ComplexbiologyChlorophyll AReproductionPhotosystem II Protein Complexfood and beveragesNADH Dehydrogenasebiology.organism_classificationChloroplastPhenotypechemistryChlorophyllThylakoidBiophysicsNew Phytologist
researchProduct

De-epoxidation of Violaxanthin in Light-harvesting Complex I Proteins

2004

The conversion of violaxanthin (Vx) to zeaxanthin (Zx) in the de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of chloroplasts against photooxidative damage. Vx is bound to the antenna proteins of both photosystems. In photosystem II, the formation of Zx is essential for the pH-dependent dissipation of excess light energy as heat. The function of Zx in photosystem I is still unclear. In this work we investigated the de-epoxidation characteristics of light-harvesting complex proteins of photosystem I (LHCI) under in vivo and in vitro conditions. Recombinant LHCI (Lhcal-4) proteins were reconstituted with Vx and lutein, and the convertibility of Vx wa…

ChlorophyllLuteinPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesXanthophyllsPhotosystem IThylakoidsBiochemistrychemistry.chemical_compoundSolanum lycopersicumSpinacia oleraceaEscherichia coliMolecular BiologyPhotosystemchemistry.chemical_classificationBinding SitesPhotosystem I Protein ComplexChemistryfood and beveragesPigments BiologicalCell Biologybeta CaroteneRecombinant ProteinsChloroplastKineticsBiochemistryXanthophyllThylakoidEpoxy CompoundsApoproteinsViolaxanthinJournal of Biological Chemistry
researchProduct

Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-…

2007

Photosynthetic light-harvesting complexes (LHCs) are assembled from apoproteins (Lhc proteins) and non-covalently attached pigments. Despite a considerable amino acid sequence identity, these proteins differ in their oligomerization behavior. To identify the amino acid residues determining the heterodimerization of Lhca1 and Lhca4 to form LHCI-730, we mutated the poorly conserved second transmembrane helix of the two subunits. Mutated genes were expressed in Escherichia coli and the resultant proteins were refolded in vitro and subsequently analyzed by gel electrophoresis. Replacement of the entire second helix in Lhca4 by the one of Lhca3 abolished heterodimerization, whereas it had no eff…

ChlorophyllModels MolecularMolecular Sequence DataLight-Harvesting Protein ComplexesBiologyProtein Structure SecondarySerineSolanum lycopersicumStructural BiologyChlorophyll bindingConsensus sequenceHistidineHomology modelingAmino Acid SequenceAmino AcidsProtein Structure QuaternaryMolecular BiologyPeptide sequenceHistidinePlant Proteinschemistry.chemical_classificationPhotosystem I Protein ComplexAmino acidTransmembrane domainProtein SubunitschemistryBiochemistryMutagenesisChlorophyll Binding ProteinsDimerizationSequence AlignmentJournal of molecular biology
researchProduct

Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
researchProduct

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