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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
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Random mutations directed to transmembrane and loop domains of the light-harvesting chlorophyll a/b protein: impact on pigment binding.

1999

The major light-harvesting complex of photosystem II (LHCII) can be reconstituted in vitro by folding its bacterially expressed apoprotein, Lhcb, in detergent solution in the presence of chlorophylls and carotenoids. To compare the impact of alpha-helical transmembrane domains and hydrophilic loop domains of the apoprotein on complex formation and stability, we introduced random mutations into a segment of the protein comprising the stromal loop, the third (C-proximal) transmembrane helix, and part of the amphipathic helix in the C-terminal domain. The mutant versions of Lhcb were screened for the loss of their ability to form stable LHCII upon reconstitution in vitro. Most steps during the…

Chlorophyll bChlorophyllProtein FoldingPigment bindingMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureChlorophyll bindingAmino Acid SequencePeptide sequencePeasMembrane ProteinsPhotosystem II Protein ComplexCarotenoidsTransmembrane proteinProtein Structure TertiaryTransmembrane domainSpectrometry FluorescencechemistryBiochemistryEnergy TransferMutationMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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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
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Exchange of Pigment-Binding Amino Acids in Light-Harvesting Chlorophyll a/b Protein

1999

Four amino acids in the major light-harvesting chlorophyll (Chl) a/b complex (LHCII) that are thought to coordinate Chl molecules have been exchanged with amino acids that presumably cannot bind Chl. Amino acids H68, Q131, Q197, and H212 are positioned in helixes B, C, A, and D, respectively, and, according to the LHCII crystal structure [Kühlbrandt, W., et al. (1994) Nature 367, 614-621], coordinate the Chl molecules named a(5), b(6), a(3), and b(3). Moreover, a double mutant was analyzed carrying exchanges at positions E65 and H68, presumably affecting Chls a(4) and a(5). All mutant proteins could be reconstituted in vitro with pigments, although the thermal stability of the resulting mut…

ChlorophyllChloroplastsMacromolecular SubstancesStereochemistryMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesTrimerBiochemistrychemistry.chemical_compoundAmino Acid SequenceAmino AcidsPeptide sequencePlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll APeasPhotosystem II Protein Complexfood and beveragesAmino acidChloroplastB vitaminsAmino Acid SubstitutionchemistryChlorophyllThylakoidMutagenesis Site-DirectedCarrier ProteinsBiochemistry
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Carotenoid binding sites in LHCIIb

2000

The major light-harvesting complex of photosystem II can be reconstituted in vitro from its bacterially expressed apoprotein with chlorophylls a and b and neoxanthin, violaxanthin, lutein, or zeaxanthin as the only xanthophyll. Reconstitution of these one-carotenoid complexes requires low-stringency conditions during complex formation and isolation. Neoxanthin complexes (containing 30–50% of the all-trans isomer) disintegrate during electrophoresis, exhibit a largely reduced resistance against proteolytic attack; in addition, energy transfer from Chl b to Chl a is easily disrupted at elevated temperature. Complexes reconstituted in the presence of either zeaxanthin or lutein contain nearly …

ChlorophyllLuteinPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesXanthophyllsBiologyBinding CompetitiveBiochemistrySubstrate SpecificityLight-harvesting complexchemistry.chemical_compoundNeoxanthinZeaxanthinsTrypsinProtein PrecursorsCarotenoidPlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll ALuteinPhotosystem II Protein Complexfood and beveragesPigments BiologicalPlantsbeta CaroteneCarotenoidseye diseasesZeaxanthinEnergy TransferchemistryBiochemistryXanthophyllElectrophoresis Polyacrylamide GelApoproteinsViolaxanthinEuropean Journal of Biochemistry
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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
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Structural and Functional Analysis of the Antiparallel Strands in the Lumenal Loop of the Major Light-harvesting Chlorophyll a/b Complex of Photosyst…

2007

The light-harvesting chlorophyll a/b-binding protein of photosystem II (LHCIIb) fulfills multiple functions, such as light harvesting and energy dissipation under different illuminations. The crystal structure of LHCIIb at the near atomic resolution reveals an antiparallel strands structure in the lumenal loop between the transmembrane helices B/C. To study the structural and functional significances of this structure, three amino acids (Val-119, His-120, and Ser-123) in this region have been exchanged to Phe, Leu, and Gly, respectively, and the influence of the mutagenesis on the structure and function of LHCIIb has been investigated. The results are as follows. 1) Circular dichroism spect…

ChlorophyllModels MolecularCircular dichroismPhotosystem IIRecombinant Fusion ProteinsLight-Harvesting Protein ComplexesAntiparallel (biochemistry)BiochemistryFluorescencechemistry.chemical_compoundNeoxanthinSite-directed mutagenesisMolecular BiologyPlant ProteinsPhotobleachingChemistryChlorophyll ACircular DichroismPeasPhotosystem II Protein ComplexCell BiologyFluorescenceTransmembrane domainB vitaminsCrystallographyMutationMutagenesis Site-DirectedProtein BindingJournal of Biological Chemistry
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Biosystematic studies on the genus Polygonatum (Convallariaceae) IV. Molecular phylogenetic analysis based on restriction site mapping of the chlorop…

1997

Phylogenetic relationships of 14 species and one variety of the genus Polygonatum as well as three species of the genus Disporopsis and Heteropolygonatum roseolum were analyzed based on mapped restriction site variation in a PCR-amplified chloroplast genome region, trnK. In agreement with earlier taxonomic treatments it was found that Disporopsis and Heteropolygonatum should be distinguished from Polygonatum at generic level, and that P. sect. Polygonatum can be recognized as a monophyletic group. Earlier series concepts in P. sect. Polygonatum based on chromosome number and characteristics of staminal filaments are not supported by the molecular data. The molecular data suggest that satell…

ChloroplastPolygonatumRestriction sitebiologyPhylogenetic treeConvallariaceaeGenusBotanyPlant Sciencebiology.organism_classificationGeneEcology Evolution Behavior and SystematicsFeddes Repertorium
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Evaluation of enantioselective binding of antihistamines to human serum albumin by ACE.

2007

The drug binding to plasma and tissue proteins is a fundamental factor in determining the overall pharmacological activity of a drug. HSA, together with alpha(1)-acid glycoprotein, are the most important plasma proteins, which act as drug carriers, with implications on the pharmacokinetic of drugs. Among plasma proteins, HSA possesses the highest enantioselectivity. In this paper, a new methodology for the study of enantiodifferentiation of chiral drugs with HSA is developed and applied to evaluate the possible enantioselective binding of four antihistamines: brompheniramine, chlorpheniramine, hydroxyzine and orphenadrine to HSA. This study includes the determination of affinity constants o…

ChlorpheniramineClinical BiochemistryPlasma protein bindingPharmacologyBiochemistryAnalytical ChemistryPharmacokineticsOrphenadrinemedicineOrphenadrineHumansSerum AlbuminDrug CarriersChromatographyBinding SitesChemistryBiological activityStereoisomerismBrompheniramineHuman serum albuminBrompheniraminebody regionsHydroxyzineembryonic structuresHistamine H1 AntagonistsEnantiomerDrug carriermedicine.drugProtein BindingElectrophoresis
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Displacement of phenprocoumon (Marcumar) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid.

1972

The technique of Sephadex gel filtration was employed to characterize the effect of some sulfonylurea compounds, ioglycamic acid, and suramin on the binding of phenprocoumon to bovine serum albumin.

ChlorpropamideChlorpropamideSuraminTolbutamideSerum albuminSuraminIn Vitro TechniquesBenzoatesPhenprocoumonCoumarinsBenzyl CompoundsmedicineAnimalsBovine serum albuminPharmacologyChromatographyBinding SitesbiologyChemistryAlbuminAnticoagulantsDextransSerum Albumin BovineGeneral MedicineCarbutamideGlycolatesCarbutamideSulfonylurea CompoundsSephadexbiology.proteinChromatography GelIodobenzoatesCattlemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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