Search results for "Electron Spin Resonance Spectroscopy"

showing 10 items of 125 documents

Experimental and Theoretical Studies on Magnetic Exchange in Silole-Bridged Diradicals.

2006

International audience; Five bis(tert-butylnitroxide) diradicals connected by a silole [2,5-R2-3,4-diphenylsilole; R = Me3CN(®O.bul.)Z; Z = p-C6H4 (7a), p-C6H4C6H4-p (7b), 1,4-naphthalenediyl (7c), m-C6H4 (7d)] or a thiophene [2,5-R2-thiophene; R = p-Me3CN(®O.bul.)C6H4 (12)] ring as a coupler were studied. Compd. 12 crystallizes in the orthorhombic space group Pna21 with a 20.752(5), b 5.826(5), and c 34.309(5) .ANG.. X-ray crystal structure detn., electronic spectroscopy, variable-temp. EPR spectroscopy, SQUID measurements and DFT computations (UB3LYP/6-31+G*) were used to study the mol. conformations and electronic spin coupling in this series of mols. Whereas compds. 7b, 7c, and 7d are q…

Models MolecularFree RadicalsSiloleCrystal structure010402 general chemistryRing (chemistry)01 natural sciencesDFTCatalysislaw.inventionchemistry.chemical_compoundNitroxide diradicalMagnetic interactionslawComputational chemistryThiopheneAntiferromagnetismOrganosilicon CompoundsSinglet stateTriplet stateElectron paramagnetic resonance010405 organic chemistryChemistry[CHIM.ORGA]Chemical Sciences/Organic chemistryOrganic ChemistryElectron Spin Resonance SpectroscopyGeneral Chemistry0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCrystallographyModels ChemicalButanesDiamagnetismEPR spectroscopy
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Heme Binding Constricts the Conformational Dynamics of the Cytochrome b559′ Heme Binding Cavity

2012

Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. The PsbF polypeptide can dimerize in the absence and presence of heme. To monitor structural alterations associated with binding of heme to the apo-cytochrome, we analyzed the apo- and holo-cytochrome structure by electron paramagnetic resonance spectroscopy. Spin labeling of amino acids located close to the heme binding domain of the cytochrome revealed that the structure of the heme binding domain is unconstrained in the absence of heme. Heme binding restricts the conformational dynamics of the heme binding domain, resulting in the structu…

Models MolecularHemeproteinCytochromeHeme bindingMolecular Sequence DataHemePlasma protein bindingBiochemistryProtein Structure SecondaryCofactorchemistry.chemical_compoundApoenzymesAmino Acid SequenceGlycophorinsHemebiologyCytochrome bCell MembraneElectron Spin Resonance SpectroscopyTemperaturePhotosystem II Protein ComplexSite-directed spin labelingCytochrome b GroupProtein Structure Tertiarychemistrybiology.proteinBiophysicsSpin LabelsPeptidesProtein BindingBiochemistry
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Synyhesis, structure, spectroscopy and redox chemistry of square-planar nickel(II) complexes with tetradentate o-phenylenedioxamidates and related li…

2005

[EN] A series of four-coordinate square-planar nickel(II) complexes of o-phenylenebis(N¿-methyloxamidate) (L1) and related o-phenylene(N¿-methyloxamidate)oxamate (L2) and o-phenylenebis(oxamate) (L3) tetradentate ligands have been synthesized and characterized structurally, spectroscopically and electrochemically. The parent nickel(II)¿L1 complex presents an intense MLCT band in the UV region (¿max = 357 nm) and a distinctive 1 s ¿ 4p CT satellite in the Ni K-edge XANES spectrum (E = 8339.2 eV). These features together with the short Ni¿N(amidate) bond lengths (1.85¿1.93 Å) as revealed by the analysis of the Ni K-edge EXAFS spectrum and confirmed by single-crystal X-ray diffraction are typi…

Models MolecularMagnetic Resonance SpectroscopySpectrophotometry Infraredchemistry.chemical_elementPhenylenediaminesCrystallography X-RayLigandsPhotochemistrySensitivity and SpecificityRedoxlaw.inventionInorganic Chemistrychemistry.chemical_compoundNickellawElectrochemistryOrganometallic CompoundsMoleculeAcetonitrileElectron paramagnetic resonanceOxalatesMolecular StructureExtended X-ray absorption fine structureLigandElectron Spin Resonance SpectroscopySpectrometry X-Ray EmissionStereoisomerismBond lengthNickelCrystallographychemistryFISICA APLICADASpectrophotometry UltravioletOxidation-Reduction
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Site-specific Labelling with a Metal Chelator for Protein-structure Refinement

2004

A single free Cys sidechain in the N-terminal domain of the E. coli arginine repressor was covalently derivatized with S-cysteaminyl-EDTA for site-specific attachment of paramagnetic metal ions. The effects of chelated metal ions were monitored with (15)N-HSQC spectra. Complexation of Co(2+), which has a fast relaxing electron spin, resulted in significant pseudocontact shifts, but also in peak doubling which was attributed to the possibility of forming two different stereoisomers of the EDTA-Co(2+) complex. In contrast, complexation of Cu(2+) or Mn(2+), which have slowly relaxing electron spins, did not produce chemical shift changes and yielded self-consistent sets of paramagnetic relaxat…

Models MolecularMagnetic Resonance SpectroscopyTime FactorsMetal ions in aqueous solutionElectronsGadoliniumBiochemistryIonParamagnetismchemistry.chemical_compoundNuclear magnetic resonanceBacterial ProteinsAmideEscherichia coliChelationCysteineEdetic AcidSpectroscopyChelating AgentsIonsManganeseElectronic correlationChemistryRelaxation (NMR)Electron Spin Resonance SpectroscopyProteinsCobaltDNAProtein Structure TertiaryRepressor ProteinsCrystallographyModels ChemicalCovalent bondProtonsCopperJournal of Biomolecular NMR
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Fluidity of liposome membranes doped with metalloporphyrins: An ESR study

2008

Changes in membrane fluidity of porphyrin-doped liposomes have been investigated to assess the kinetics of the fluidization process. Metal complexes of tert-butylphenyl mesosubstituted porphyrin, containing ions of Mg, Mn, Fe, Co, Ni and Cu, were used as dopants. Liposomes were obtained by sonication of hen egg yolk lecithin (EYL). Electron paramagnetic resonance (ESR) was applied using two spin probes, TEMPO (2,2,6,6-tetramethylpiperidine- 1-oxyl) and 16-DOXYL-stearic acid [2-ethyl-2-(15-methoxy-15-oxopentadecyl)-4,4- dimethyl-3-oxazolidinyloxyl], localized at different sites within the membrane to determine the spectroscopic parameters: partition (F) and rotation correlation time (τ), rel…

Models MolecularMembrane FluidityMetalloporphyrinsSonicationInorganic chemistryKineticsMolecular ConformationGeneral Biochemistry Genetics and Molecular Biologylaw.inventionEYL LiposomesMetalCyclic N-Oxideschemistry.chemical_compoundlawMembrane fluidityElectron paramagnetic resonanceESRLiposomeChemistryElectron Spin Resonance SpectroscopyPorphyrinKineticsMembranevisual_artLiposomesvisual_art.visual_art_mediumSpin Labels
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Oxidation of substituted phenols using copper(II) metallatriangles formed through ligand sharing

2014

Reaction of N(2),N(2')-bis-[(1-butyl-benzimidazol-2yl)methyl]biphenyl-2,2'-dicarboxamide (L) with CuX2⋅nH2O in methanol leads to the assembly of four trinuclear Cu(II) complexes with the general formula [Cu3(L)3X3]⋅3X⋅nH2O⋅mMeCN, where X=Cl(-), Br(-), NO3(-) and C6H5COO(-) and n=0-5, m=0-8 (compounds 1-4, respectively). The structure of one of the complex contains three Cu(II) metal ions at the corners of an equilateral triangle. Each of the copper(II) are coordinated through two benzimidazolyl imine N-atoms and two amide carbonyl O-atoms and the apical position is occupied by an anionic nitrate ion, leading to a distorted square pyramidal environment. The magnetic susceptibility data were …

Models MolecularMetal ions in aqueous solutionInorganic chemistryIminechemistry.chemical_elementLigandsMedicinal chemistryAnalytical ChemistryMagneticschemistry.chemical_compoundPhenolsAmidePhenolsInstrumentationSpectroscopyDiamideElectron Spin Resonance SpectroscopyCopperAtomic and Molecular Physics and OpticsSquare pyramidal molecular geometryQuinonechemistryBenzimidazolesOxidation-ReductionPhenoxazineCopperSpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
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Co(II) chemistry of 2,6-bis(2-pyridylcarbonyl)pyridine: an icosanuclear Co cluster exhibiting superparamagnetic relaxation.

2006

High-nuclearity transition-metal complexes (clusters) are of special interest in chemistry and physics because, both in terms of size and physical properties, they bridge the gap between the microscopic and macroscopic world, and between quantum and classical systems. In terms of size, the smallest classical nanoparticles fabricated today are the same size as the largest metal clusters that are synthesized by bottom-up methods. In terms of physical properties, certain transition-metal clusters exhibit single-molecule magnetism at low temperatures, that is, they retain their magnetization in zero field in a manner analogous to that of classical macroscopic magnets, but at the same time they …

Models MolecularMolecular StructureChemistryMagnetismStereochemistryPyridinesRelaxation (NMR)Electron Spin Resonance SpectroscopyTemperatureStereoisomerismGeneral MedicineGeneral ChemistryCobaltCrystallography X-RayLigandsCatalysisMagnetizationMagneticsChemical physicsCluster (physics)Organometallic CompoundsQuantumQuantum tunnellingSuperparamagnetismQuantum computerAngewandte Chemie (International ed. in English)
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Metalloporphyrin intercalation in liposome membranes: ESR study

2010

Liposomes characterized by membranes featuring diverse fluidity (liquid-crystalline and/or gel phase), prepared from egg yolk lecithin (EYL) and dipalmitoylphosphatidylcholine (DPPC), were doped with selected metalloporphyrins and the time-related structural and dynamic changes within the lipid double layer were investigated. Porphyrin complexes of Mg(II), Mn(III), Fe(III), Co(II), Ni(II), Cu(II), Zn(II), and the metal-free base were embedded into the particular liposome systems and tested for 350 h at 24°C using the electron spin resonance (ESR) spin probe technique. 5-DOXYL, 12-DOXYL, and 16-DOXYL stearic acid methyl ester spin labels were applied to explore the interior of the lipid bila…

Models MolecularOriginal PaperLiposomeMolecular StructureMetalloporphyrinsIntercalation (chemistry)Electron Spin Resonance SpectroscopyPorphyrinBiochemistryLipid bilayerSpin probeInorganic Chemistrychemistry.chemical_compoundCrystallographyMembranechemistryElectron spin resonanceDipalmitoylphosphatidylcholineLiposomesDensity functional theory calculationsOrganic chemistrylipids (amino acids peptides and proteins)Lipid bilayer phase behaviorLipid bilayerJBIC Journal of Biological Inorganic Chemistry
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Dynamics of surface of lipid membranes: theoretical considerations and the ESR experiment.

2016

The effect of the surface layer of model membranes on their physical properties was discussed in this paper. The research involved a physical ESR experiment with the use of spin probes and computer simulation based on the Monte Carlo technique. Liposomes formed during the process of sonication of lecithin were scanned in an ESR spectrometer. The membrane surface layer model, represented by the system of electric dipoles arranged in rectangular or hexagonal matrices, was studied. The final states of computer simulations were presented as textures. It was found that in the gel phase some ordered domain structures are formed, while in the liquid–crystal phase we got complex textures comprising…

Models MolecularPhase transition12-DipalmitoylphosphatidylcholineSurface PropertiesMonte Carlo methodBiophysicsAnalytical chemistryMolecular Conformation02 engineering and technologyPhase Transition03 medical and health sciencesSonication0302 clinical medicinePhase (matter)Lipid membraneSurface layerMembrane fluidityLipid bilayerMonte Carlo simulationChemistryCell MembraneElectron Spin Resonance SpectroscopyTemperatureGeneral MedicineHydrogen-Ion ConcentrationESR probe021001 nanoscience & nanotechnologyElectric dipole momentDipoleKineticsMembraneChemical physics030220 oncology & carcinogenesisLiposomesOriginal Article0210 nano-technologyMonte Carlo MethodEuropean biophysics journal : EBJ
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Characterization of phenolic pellets for ESR dosimetry in photon beam radiotherapy

2017

This work deals with the dosimetric features of a particular phenolic compound (IRGANOX 1076 ® ) for dosimetry of clinical photon beams by using electron spin resonance (ESR) spectroscopy. After the optimization of the ESR readout parameters (namely modulation amplitude and microwave power) to maximise the signal without excessive spectrum distortions, basic dosimetric properties of laboratory-made phenolic dosimeters in pellet form, such as reproducibility, dose–response, sensitivity, linearity and dose rate dependence were investigated. The dosimeters were tested by measuring the depth dose profile of a 6 MV photon beam. A satisfactory intra-batch reproducibility of the ESR signal of the …

Models MolecularPhotonBiophysicsMolecular ConformationIRGANOX 1076 ®RadiationSignal030218 nuclear medicine & medical imaging03 medical and health sciences0302 clinical medicineNuclear magnetic resonancePhenolsDosimetryDosimetrySpectroscopyMicrowavesRadiometryGeneral Environmental ScienceESRReproducibilityPhotonsDosimeterRadiationPhenolRadiotherapy2300ChemistryElectron Spin Resonance SpectroscopyRadiotherapy DosagePhotonBiophysic030220 oncology & carcinogenesisMicrowaveMicrowave
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