0000000000082182

AUTHOR

Franz-josef Schmitt

showing 10 related works from this author

Surface functionalization and surface recognition: Plasmon optical detection of molecular recognition at self assembled monolayers

1991

The synthesis of biotin- functionalized organic mercaptans and their chemisorption on gold surfaces is described. Biotin bound covalently to self assembled monolayers is recognized by streptavidin from aqueous buffer solutions. Spacer length and packing density of the biotin labels on the organic surface determine the docking kinetics. With a flexible and hydrophilic spacer very fast -diffusion controlled-docking is observed. As an alternative method of self assembly the spreading of organic mercaptans on water surfaces is established. Pressure-area diagrams of different functionalized mercaptans and disulfides are shown and their monolayer properties are discussed.

StreptavidinPolymers and PlasticsChemistryOrganic ChemistrySelf-assembled monolayerCondensed Matter PhysicsCombinatorial chemistrychemistry.chemical_compoundMolecular recognitionChemisorptionMonolayerMaterials ChemistryOrganic chemistrySurface modificationSelf-assemblyPlasmonMakromolekulare Chemie. Macromolecular Symposia
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Excitonic energy level structure and pigment-protein interactions in the recombinant water-soluble chlorophyll protein. II. Spectral hole-burning exp…

2011

Persistent spectral hole burning at 4.5 K has been used to investigate the excitonic energy level structure and the excited state dynamics of the recombinant class-IIa water-soluble chlorophyll-binding protein (WSCP) from cauliflower. The hole-burned spectra are composed of four main features: (i) a narrow zero-phonon hole (ZPH) at the burn wavelength, (ii) a number of vibrational ZPHs, (iii) a broad low-energy hole at ~665 and ~683 nm for chlorophyll b- and chlorophyll a-WSCP, respectively, and (iv) a second satellite hole at ~658 and ~673 nm for chlorophyll b- and chlorophyll a-WSCP, respectively. The doublet of broad satellite holes is assigned to an excitonically coupled chlorophyll dim…

ChlorophyllChlorophyll aExcitonAnalytical chemistryLight-Harvesting Protein ComplexesElectronsBrassicaVibrationSpectral linechemistry.chemical_compoundMaterials ChemistryPhysical and Theoretical ChemistryPhysics::Biological PhysicsChlorophyll AWaterFluorescenceRecombinant ProteinsSurfaces Coatings and FilmsWavelengthSpectrometry FluorescencechemistryExcited stateChlorophyllSpectral hole burningThermodynamicsAtomic physicsThe journal of physical chemistry. B
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Pigment−Pigment and Pigment−Protein Interactions in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower

2007

Plants contain water-soluble chlorophyll-binding proteins (WSCPs) that function neither as antennas nor as components of light-induced electron transfer of photosynthesis but are likely constituents of regulatory protective pathways in particular under stress conditions. This study presents results on the spectroscopic properties of recombinant WSCP from cauliflower reconstituted with chlorophyll b (Chl b) alone or with mixtures of Chl a and Chl b. Two types of experiments were performed: (a) measurements of stationary absorption spectra at 77 and 298 K and CD spectra at 298 K and (b) monitoring of laser flash-induced transient absorption changes with a resolution of 200 fs in the time doma…

Chlorophyll bCircular dichroismAbsorption spectroscopyCircular DichroismLasersDimerKineticsLight-Harvesting Protein ComplexesBrassicaPigments BiologicalRecombinant ProteinsSurfaces Coatings and FilmsKineticschemistry.chemical_compoundCrystallographyElectron transferchemistryUltrafast laser spectroscopyChlorinMaterials ChemistryLinear Energy TransferSpectrophotometry UltravioletPhysical and Theoretical ChemistryThe Journal of Physical Chemistry B
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Ligand-receptor interactions directly measured with the surface forces apparatus

1991

Ligand-receptor interactions give rise to very strong bonds due to perfect geometrical fit. Using the Surface Forces Apparatus we have studied the interactions between membrane-bound biotin ligands and streptavidin receptors. We find an unusually strong short-range binding force associated with equally specific molecular rearrangements-both qualitatively and quantitatively unlike anything previously measured.

Streptavidinchemistry.chemical_compoundCrystallographyPolymers and PlasticschemistryBiotinLigandOrganic ChemistryMaterials ChemistrySurface forces apparatusCondensed Matter PhysicsReceptorBinding forceMakromolekulare Chemie. Macromolecular Symposia
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Molecular mechanisms determining the strength of receptor-mediated intermembrane adhesion

1995

The strength of receptor-mediated cell adhesion is directly controlled by the mechanism of cohesive failure between the cell surface and underlying substrate. Unbinding can occur either at the locus of the specific bond or within the bilayer, which results in tearing the hydrophobic anchors from the membrane interior. In this work, the surface force apparatus has been used to investigate the relationship between the receptor-ligand bond affinities and the dominant mechanism of receptor-coupled membrane detachment. The receptors and ligands used in this study were membrane-bound streptavidin and biotin analogs, respectively, with solution affinities ranging over 10 orders of magnitude. With …

StreptavidinStereochemistryLipid BilayersMolecular ConformationBiophysicsReceptors Cell Surface02 engineering and technologyModels BiologicalCell membrane03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsmedicineCell AdhesionAnimalsBond energyLipid bilayer030304 developmental biologyFluorescent Dyes0303 health sciencesThioctic AcidBilayerPhosphatidylethanolaminesCell MembraneSurface forces apparatus021001 nanoscience & nanotechnologyAffinitiesModels StructuralKineticsmedicine.anatomical_structureMembranechemistryBiophysicsStreptavidin0210 nano-technologyAzo CompoundsResearch ArticleBiophysical Journal
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Water soluble chlorophyll binding protein of higher plants: A most suitable model system for basic analyses of pigment–pigment and pigment–protein in…

2011

Abstract This short review paper describes spectroscopic studies on pigment–pigment and pigment–protein interactions of chlorophyll (Chl) a and b bound to the recombinant protein of class IIa water soluble chlorophyll protein (WSCP) from cauliflower. Two Chls form a strongly excitonically coupled open sandwich dimer within the tetrameric protein matrix. In marked contrast to the mode of excitonic coupling of Chl and bacterio-Chl molecules in light harvesting complexes and reaction centers of all photosynthetic organisms, the unique structural pigment array in the Chl dimer of WSCP gives rise to an upper excitonic state with a large oscillator strength. This property opens the way for thorou…

ChlorophyllPhysiologyTetrameric proteinDimerLight-Harvesting Protein ComplexesTemperatureWatermacromolecular substancesPlant SciencePlantsPhotochemistryPhotosynthesisModels BiologicalLight-harvesting complexchemistry.chemical_compoundPigmentchemistryChlorophyllvisual_artvisual_art.visual_art_mediumChlorophyll bindingMoleculeAgronomy and Crop ScienceJournal of Plant Physiology
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Thermally Activated Superradiance and Intersystem Crossing in the Water-Soluble Chlorophyll Binding Protein

2009

The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests that both types of WSCP share a common Chl binding motif, where the opening angle between pigment planes in class IIa WSCP should not differ by more than 10 degrees from that in class IIb. The experimentally observed (Schmitt et al. J. Phys. Chem. B 2008, 112, 13951) decrease in excited state lifetime of Chl a homodimers with increasing …

Models MolecularCircular DichroismDimerExcitonStatic ElectricityLight-Harvesting Protein ComplexesTemperatureWaterCrystal structureCrystallography X-RayPhotochemistryLepidiumSurfaces Coatings and Filmschemistry.chemical_compoundCrystallographyIntersystem crossingSolubilitychemistryChlorophyllExcited stateMaterials ChemistryChlorophyll bindingQuantum TheoryPhysical and Theoretical ChemistryAbsorption (chemistry)The Journal of Physical Chemistry B
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Specific Protein Binding to Functionalized Interfaces

1992

We report on the characterization of specific binding reactions between streptavidin and biotinylated model membrane surfaces. Self-assembly techniques as well as the Langmuir-Blodgett-Kuhn method were employed to prepare reactive, functionalized surfaces on various solid supports in contact with the aqueous protein solution. Plasmon surface polaritons optical measurements as well as atomic force microscopy and studies with the surface forces apparatus give rather detailed information as to the streptavidin monolayer formation, the kinetics of this process (either binding site- or diffusion limited), the selectivity of the reaction at laterally heterogeneous membranes, and the involved inte…

Streptavidinchemistry.chemical_compoundAqueous solutionMembraneChemistryBiotinylationMonolayerSurface forces apparatusBinding siteCombinatorial chemistryPlasmon
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Specific dye adsorption at oriented monolayers

2007

We studied the adsorption of water soluble cyanine dyes (pseudoiso-cyanine and “stains-all”) to monomolecular layers of arachidic acid at the water-air interface in a Langmuir trough. Fluorescence microscopy was employed to on-line monitor the formation of J-aggregates upon adsorption. Large two-dimensional monodomain single crystals could be grown by this self-assembly process with optical properties reminiscent of those found and extensively studied for amphiphilic derivatives of the same chromophors [12]. In addition to the necessary Coulombic interaction between subphasedye and target monolayer, we found that details of the crystal morphology also crucially depend on substrate parameter…

chemistry.chemical_compoundMaterials scienceAdsorptionchemistryAbsorption spectroscopyChemical engineeringDesorptionMicroscopyMonolayerArachidic acidCyanineFluorescence spectroscopy
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Excited State Dynamics in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower Investigated by Transient Fluorescence Spectroscopy

2008

The present study describes the fluorescence emission properties of recombinant water-soluble chlorophyll (Chl) protein (WSCP) complexes reconstituted with either Chl a or Chl b alone (Chl a only or Chl b only WSCP, respectively) or mixtures of both pigments at different stoichiometrical ratios. Detailed investigations were performed with time and space correlated ps fluorescence spectroscopy within the temperature range from 10 to 295 K. The following points were found: (a) The emission spectra at room temperature (295 K) are well characterized by bands with a dominating Lorentzian profile broadened due to phonon scattering and peak positions located at 677, 684 and 693 nm in the case of C…

Time FactorsLight-Harvesting Protein ComplexesTemperatureAnalytical chemistryWaterBrassicaAtmospheric temperature rangeFluorescenceRecombinant ProteinsSpectral lineFluorescence spectroscopySurfaces Coatings and FilmsPigmentchemistry.chemical_compoundSpectrometry FluorescenceSolubilitychemistryvisual_artExcited stateChlorophyllMaterials Chemistryvisual_art.visual_art_mediumEmission spectrumPhysical and Theoretical ChemistryPlant ProteinsThe Journal of Physical Chemistry B
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