Search results for "Protoporphyrin"

showing 10 items of 37 documents

Spectral hole burning study of protoporphyrin IX substituted myoglobin.

1992

Protoporphyrin IX substituted myoglobin reveals excellent hole burning properties. We investigated the frequency shift of persistent spectral holes under isotropic pressure conditions in a range from 0 to 2.4 MPa. In this range, the protein behaves like an elastic solid. The shift of the holes under pressure shows a remarkable frequency dependence from which the compressibility of the protein can be determined. The compressibility, in turn, allows for an estimation of the equilibrium volume fluctuations. Within the frame of the model used to interpret the pressure data, it is possible to determine the absorption frequency of the isolated chromophore and the associated solvent shift in the p…

Quantitative Biology::BiomoleculesProtoporphyrin IXMyoglobinPhotochemistryProtein ConformationAnalytical chemistryFluorescence spectrometryBiophysicsProtoporphyrinsChromophorechemistry.chemical_compoundSpectrometry FluorescencechemistryMyoglobinSpectral hole burningCompressibilityAnimalsProtoporphyrinHorsesCompressibility factorResearch ArticleBiophysical journal
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Effects of peroxidizing herbicides on protoporphyrin IX levels in non-chlorophyllous soybean cell culture

1990

Abstract The mode of action of 16 peroxidizing herbicides belonging to four different families (diphenyl ethers, oxadiazon, pyridine derivatives, and pyrazole derivatives) has been studied in nonchlorophyllous soybean cell cultures. Whenever possible, we have compared active and inactive compounds. Phytotoxic effects were estimated on the basis of growth inhibition, either in the dark or in the light. Protoporphyrin IX accumulations were estimated in dark-treated samples, using a simple methodology. In all cases, we have found a positive correlation between cellular damages and protoporphyrin IX accumulations. The results provide further evidences in favor of the light-dependent activity of…

0106 biological sciences0303 health sciencesProtoporphyrin IXChemistryHealth Toxicology and Mutagenesis[SDV]Life Sciences [q-bio]General MedicineMetabolismPyrazole01 natural sciencesPorphyrin[SDV] Life Sciences [q-bio]03 medical and health scienceschemistry.chemical_compoundTissue cultureBiochemistryProtoporphyrinGrowth inhibitionMode of actionAgronomy and Crop Science030304 developmental biology010606 plant biology & botany
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Hole burning and pressure phenomena in chromoproteins

1993

Abstract We investigated the behavior of spectral holes under pressure at various frequencies within the inhomogeneous band for two proteins, namely myoglobin and horseradish peroxidase. In order to achieve narrow bandwidth hole burning, the heme chromophore was replaced by protoporphyrin IX and mesoporphyrin IX, respectively. In myoglobin, we found that the pressure induced shift of the holes varied in a strongly non-linear fashion, when the burn-frequency was tuned across the absorption band. In horseradish peroxidase the pressure shift was linear with burn-frequency but changed in a dramatic fashion upon complex formation with a substrate molecule. These observations are interpreted with…

HemeproteinbiologyProtoporphyrin IXChemistryBiophysicsGeneral ChemistryChromophoreCondensed Matter PhysicsPhotochemistryBiochemistryHorseradish peroxidaseMolecular physicsAtomic and Molecular Physics and Opticschemistry.chemical_compoundMyoglobinAbsorption bandbiology.proteinHemePeroxidaseJournal of Luminescence
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X-linked protoporphyria: Iron supplementation improves protoporphyrin overload, liver damage and anaemia

2015

0301 basic medicinemedicine.medical_specialtybusiness.industryHematologymedicine.disease03 medical and health sciencesLiver diseasechemistry.chemical_compound030104 developmental biologyEndocrinologyPorphyriachemistryInternal medicineHaem biosynthesisIron supplementationMedicineErythropoiesisProtoporphyrinLiver damagebusinessBritish Journal of Haematology
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Synthesis and properties of a photoaffinity labeling reagent for protoporphyrinogen oxidases, the target enzymes of diphenyl ether herbicides

1994

A diazoketone 3 has been synthesized in two steps from acifluorfen 1, a diphenyl ether herbicide. Like the parent compound 1, the diazoketone 3 is toxic to plant cells and inhibits protoporphyrinogen oxidase, the molecular target of diphenyl ether herbicides. On photolysis of 3 in methanol, the generated carbene mainly undergoes the Wolff rearrangement to a ketene which further adds methanol, but many other products are observed. A tritiated derivative of 3 has been prepared which is suitable for photoaffinity labeling experiments.

0106 biological sciencesOxidoreductases Acting on CH-CH Group Donors[SDV]Life Sciences [q-bio]Clinical BiochemistryPharmaceutical ScienceKeteneAcifluorfen01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundDrug DiscoveryOrganic chemistryProtoporphyrinogen OxidaseMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesPhotolysisPhotoaffinity labelingMolecular StructureBIOCHIMIEHerbicidesOrganic ChemistryDiphenyl etherWolff rearrangementAffinity Labels[SDV] Life Sciences [q-bio]chemistryTOXICOLOGIEReagentMolecular MedicineProtoporphyrinogen oxidaseIndicators and ReagentsMethanolSoybeansOxidoreductases010606 plant biology & botany
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With a Little Help from My Friends: The Role of Intraoperative Fluorescent Dyes in the Surgical Management of High-Grade Gliomas

2018

High-grade gliomas (HGGs) are the most frequent primary malignant brain tumors in adults, which lead to death within two years of diagnosis. Maximal safe resection of malignant gliomas as the first step of multimodal therapy is an accepted goal in malignant glioma surgery. Gross total resection has an important role in improving overall survival (OS) and progression-free survival (PFS), but identification of tumor borders is particularly difficult in HGGS. For this reason, imaging adjuncts, such as 5-aminolevulinic acid (5-ALA) or fluorescein sodium (FS) have been proposed as superior strategies for better defining the limits of surgical resection for HGG. 5-aminolevulinic acid (5-ALA) is i…

Oncologymedicine.medical_specialtyReviewlcsh:RC321-571Resection03 medical and health scienceschemistry.chemical_compoundHigh-grade glioma0302 clinical medicineGliomaInternal medicineYELLOW 560 filterMedicinefluorescein sodiumastrocytomalcsh:Neurosciences. Biological psychiatry. NeuropsychiatryProtoporphyrin IXSettore MED/27 - Neurochirurgiabusiness.industryGeneral NeuroscienceglioblastomaAstrocytomaMultimodal therapymedicine.diseaseFluorescenceextent of resectionchemistry5-aminolevulinic acid030220 oncology & carcinogenesisPrimary Malignant Brain TumorsSodium fluoresceinbusinesshigh-grade gliomas030217 neurology & neurosurgeryBrain Sciences
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Organometallic complexes with biological molecules. I. Diorganotin(IV)chloro protoporphyrin IX complexes: Solid-state and solution-phase characteriza…

1993

Protoporphyrin IX (H4PPIX) complexes of diorganotin(IV)chloro moieties with formula (R2SnCl)2H2PPIX (RMe, Bu and Ph) have been obtained and their solid-state and solution-phase configurations have been studied through spectroscopic investigations. Coordination of the side-chain carboxylates of H4PPIX to R2Sn(IV)Cl moieties, with bridging carboxylate (COO−) has been inferred by comparison of the free and coordinated H4PPIX IR spectra, while the occurrence of a five-coordinated tin(IV) atom in a cis-R2 trigonal bipyramidal structure has been deduced, for all of the synthesized complexes, by rationalization of the nuclear quadrupole splitting parameters, according to the point-charge model for…

Protoporphyrin IXStereochemistrychemistry.chemical_elementInfrared spectroscopyGeneral ChemistryQuadrupole splittingInorganic Chemistrychemistry.chemical_compoundCrystallographyTrigonal bipyramidal molecular geometryMonomerchemistryMössbauer spectroscopyCarboxylateTinApplied Organometallic Chemistry
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Thermal broadening of the Soret band in heme complexes and in heme-proteins: role of iron dynamics

1994

We report the thermal broadening of the Soret band in heme-CO, heme-OH and protoporphyrin IX in the temperature range 300-20 K. For protoporphyrin IX the temperature dependent Gaussian line broadening follows the behavior predicted by the harmonic approximation in the entire temperature range investigated. In contrast, for heme-CO and heme-OH the harmonic behavior is obeyed only up to about 180 K and an anomalous line broadening increase is observed at higher temperatures. This effect is attributed to the onset of anharmonic motions of the iron atom with respect to the porphyrin plane. Comparison with previously reported analogous data for heme proteins enables us to suggest that the onset …

HemeproteinsHot TemperatureHemeproteinIronBiophysicsProtoporphyrinsHemePhotochemistryMolecular physicsHemoglobinschemistry.chemical_compoundAtomAnimalsHemeProtoporphyrin IXMyoglobinProtein dynamicsAnharmonicityGeneral MedicineAtmospheric temperature rangePorphyrinCarboxyhemoglobinchemistrySpectrophotometryThermodynamicsCattleEuropean Biophysics Journal
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Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen

1992

It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]PhthalimidesAcifluorfen01 natural sciencesBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEEtioplastProtoporphyrinogen OxidaseBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOrganelles0303 health sciencesOxidase testBinding SitesPlants MedicinalProtoporphyrin IXMolecular StructureBIOCHIMIEHerbicidesFabaceaeProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryBiochemistryNitrobenzoatesProtoporphyrinogen oxidaseOxidoreductases010606 plant biology & botany
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Hemin-coupled iron(III)-hydroxide nanoparticles show increased uptake in Caco-2 cells

2011

Abstract Objectives The absorption of commonly used ferrous iron salts from intestinal segments at neutral to slightly alkaline pH is low, mainly because soluble ferrous iron is easily oxidized to poorly soluble ferric iron and ferrous iron but not ferric iron is carried by the divalent metal transporter DMT-1. Moreover, ferrous iron frequently causes gastrointestinal side effects. In iron(III)-hydroxide nanoparticles hundreds of ferric iron atoms are safely packed in nanoscaled cores surrounded by a solubilising carbohydrate shell, yet bioavailability from such particles is insufficient when compared with ferrous salts. To increase their intestinal uptake iron(III)-hydroxide nanoparticles …

Inorganic chemistryTetrazolium SaltsPharmaceutical ScienceNanoparticleFerrozineIron Chelating AgentsFerric CompoundsFerrouschemistry.chemical_compoundMicroscopy Electron TransmissionSpectroscopy Fourier Transform InfraredmedicineHumansScattering RadiationParticle SizeColoring AgentsHemePharmacologyChemistryIron Chelating AgentsIron deficiencymedicine.diseaseCulture MediaThiazolesHeminNanoparticlesHydroxideColorimetrySpectrophotometry UltravioletProtoporphyrinCaco-2 CellsHeminJournal of Pharmacy and Pharmacology
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