Search results for "MYOGLOBIN"

showing 10 items of 141 documents

Combination of acoustic levitation with small angle scattering techniques and synchrotron radiation circular dichroism. Application to the study of p…

2016

Abstract Background The acoustic levitation technique is a useful sample handling method for small solid and liquids samples, suspended in air by means of an ultrasonic field. This method was previously used at synchrotron sources for studying pharmaceutical liquids and protein solutions using x-ray diffraction and small angle x-ray scattering (SAXS). Methods In this work we combined for the first time this containerless method with small angle neutron scattering (SANS) and synchrotron radiation circular dichroism (SRCD) to study the structural behavior of proteins in solutions during the water evaporation. SANS results are also compared with SAXS experiments. Results The aggregation behavi…

Neutron diffractionBiophysicsEvaporationAnalytical chemistry02 engineering and technology010402 general chemistryAcoustic levitation01 natural sciencesBiochemistrylaw.inventionlawScattering Small AngleAnimalsHorsesMolecular BiologyComputingMilieux_MISCELLANEOUSMyoglobinScatteringChemistrySmall-angle X-ray scatteringCircular DichroismSpectrum AnalysisProteinsWaterAcoustics[CHIM.MATE]Chemical Sciences/Material chemistry021001 nanoscience & nanotechnologySmall-angle neutron scatteringSynchrotron0104 chemical sciencesSolutionsNeutron DiffractionMuramidaseSmall-angle scattering0210 nano-technologyChickensSynchrotrons
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Recombination studies of photodissociated MbCO by Mössbauer spectroscopy at low temperatures

1990

Rebinding of carbonmonoxide to myoglobin after photodissociation has been studied by Mossbauer spectroscopy at 57.6 K and below for up to 9 days. The time dependence is reproduced by a set of exponentials representing a distribution of activation enthalpies. A shift to smaller values of these activation enthalpies and of the preexponential factor compared to optical studies at higher temperatures has been observed as well as pumping into long-living states.

Nuclear and High Energy PhysicsChemistryEnthalpyPhotodissociationAnalytical chemistryCondensed Matter PhysicsAtomic and Molecular Physics and Opticschemistry.chemical_compoundMyoglobinComputational chemistryMössbauer spectroscopyPhysical and Theoretical ChemistryThin filmSpectroscopyRecombinationHyperfine Interactions
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Rayleigh scattering of Mössbauer radiation on a myoglobin single crystal

1992

The RSMR technique was used to determine the fraction of radiation which is scattered elastically and inelastically, respectively, into Bragg reflections of a metmyoglobin single crystal. From this measurement 〈x2 1c〉=0.027±0.008 A2 has been determined which is due to long range correlated motions in analogy to acoustic and optic modes in solids.

Nuclear and High Energy PhysicsRange (particle radiation)Mössbauer effectChemistrybusiness.industryScatteringPhysics::OpticsBragg's lawInelastic scatteringCondensed Matter PhysicsMolecular physicsAtomic and Molecular Physics and Opticssymbols.namesakeOpticsMetmyoglobinsymbolsHigh Energy Physics::ExperimentPhysical and Theoretical ChemistryRayleigh scatteringbusinessSingle crystalHyperfine Interactions
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Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

2015

Immobilization of proteins and other biomolecules in saccharide matrices leads to a series of peculiar properties that are relevant from the point of view of both biochemistry and biophysics, and have important implications on related fields such as food industry, pharmaceutics, and medicine. In the last years, the properties of biomolecules embedded into glassy matrices and/or highly concentrated solutions of saccharides have been thoroughly investigated, at the molecular level, through in vivo, in vitro, and in silico studies. These systems show an outstanding ability to protect biostructures against stress conditions; various mechanisms appear to be at the basis of such bioprotection, th…

Organic Chemistrytrehalose protein dynamics biopreservation myoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Current Organic Chemistry
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Myoglobin, expressed in brown adipose tissue of mice, regulates the content and activity of mitochondria and lipid droplets

2021

Abstract The identification of novel physiological regulators that stimulate energy expenditure through brown adipose tissue (BAT) activity in substrate catalysis is of utmost importance to understand and treat metabolic diseases. Myoglobin (MB), known to store or transport oxygen in heart and skeletal muscles, has recently been found to bind fatty acids with physiological constants in its oxygenated form (i.e., MBO2). Here, we investigated the in vivo effect of MB expression on BAT activity. In particular, we studied mitochondrial function and lipid metabolism as essential determinants of energy expenditure in this tissue. We show in a MB-null (MBko) mouse model that MB expression in BAT i…

PalmitatesOxidative phosphorylationMitochondrion1307 Cell BiologyMiceAdipose Tissue BrownLipid dropletBrown adipose tissueRespiration1312 Molecular BiologymedicineAnimalsHumansPPAR alpha11434 Center for Clinical StudiesMuscle SkeletalMolecular BiologyUncoupling Protein 1Mice KnockoutMyoglobinChemistryProteinsThermogenesisLipid metabolismLipid DropletsCell BiologyMetabolism10081 Institute of Veterinary PhysiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaCell biologyOxygenDisease Models AnimalAdipocytes Brownmedicine.anatomical_structure10076 Center for Integrative Human Physiology570 Life sciences; biologyApoptosis Regulatory ProteinsEnergy MetabolismThermogenesisBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Failure of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ) to inhibit soluble guanylyl cyclase in rat ventricular cardiomyocytes

1999

The effects of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ), an inhibitor of soluble guanylyl cyclase (sGC), were investigated in aortic rings and ventricular cardiomyocytes from rats. The production of cyclic GMP was stimulated by NO•-donors or carbachol. Additionally, the effects of ODQ were studied in cytosolic extracts from both tissues in which the cyclic GMP production was stimulated by S-nitroso-N-acetylpenicillamine (SNAP). In endothelium-intact aortic rings, SNAP (100 μM), 2,2′-(hydroxynitrosohydrazino)bis-ethanamine (DETA NONOate; 100 μM), or carbachol (10 μM) increased cyclic GMP levels about 4 fold. These effects were abolished by ODQ (50 μM). In cardiomyocytes, SNAP (100 μ…

Pharmacologymedicine.medical_specialtyAortaCarbacholChemistrySnapIn vitroNitric oxideCytosolchemistry.chemical_compoundEndocrinologyMyoglobinInternal medicinemedicine.arterymedicineSoluble guanylyl cyclasemedicine.drugBritish Journal of Pharmacology
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Effects of nitric oxide donors on cardiac contractility in wild-type and myoglobin-deficient mice

2002

1. The effects of the nitric oxide (NO) donors S-nitroso-N-acetylpenicillamine (SNAP), sodium(Z)-1-(N,N-diethylamino)diazen-1-ium-1,2-diolate (DEA-NONOate), and (Z)-1-[N-(2-Aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolate (DETA-NONOate) on force of contraction (F(c)) were studied in atrial and ventricular muscle strips obtained from wild-type (WT) and myoglobin-deficient (myo(-/-)) mice. 2. SNAP slightly reduced F(c) in preparations from WT mice at concentrations above 100 microM; this effect was more pronounced in myo(-/-) mice. 3. DEA-NONOate reduced F(c) in preparations from myo(-/-) mice to a larger extent than those from WT mice. 4. DETA-NONOate reduced F(c) in preparations…

Pharmacologymedicine.medical_specialtyWild typeSnapNitric oxideContractilitychemistry.chemical_compoundEndocrinologychemistryMyoglobinInternal medicinemedicineSoluble guanylyl cyclaseReceptorIntracellularBritish Journal of Pharmacology
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Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy.

2015

International audience; We report time-resolved X-ray absorption measurements after photolysis of carbonmonoxy myoglobin performed at the LCLS X-ray free electron laser with nearly 100 fs (FWHM) time resolution. Data at the Fe K-edge reveal that the photoinduced structural changes at the heme occur in two steps, with a faster (∼70 fs) relaxation preceding a slower (∼400 fs) one. We tentatively attribute the first relaxation to a structural rearrangement induced by photolysis involving essentially only the heme chromophore and the second relaxation to a residual Fe motion out of the heme plane that is coupled to the displacement of myoglobin F-helix

PhotodissociationAbsorption spectroscopyTime resolved spectroscopyInvited ArticlesPhotochemistrySPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2chemistry.chemical_compoundX-ray absorption spectralcsh:QD901-999X-ray absorption near edge structureSpectroscopyInstrumentationHemeSpectroscopy[PHYS]Physics [physics]RadiationX-ray optics[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryPhotodissociationRelaxation (NMR)ChromophoreCondensed Matter PhysicsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)MyoglobinBiofisica Dinamica delle proteine Spettroscopia risolta in tempo X-ray free-electron laser Assorbimento di raggi Xlcsh:CrystallographyTime-resolved spectroscopyStructural dynamics (Melville, N.Y.)
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X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation.

1996

The x-ray structure of carbon monoxide (CO)-ligated myoglobin illuminated during data collection by a laser diode at the wavelength lambda = 690 nm has been determined to a resolution of 1.7 A at T = 36 K. For comparison, we also measured data sets of deoxymyoglobin and CO-ligated myoglobin. In the photon-induced structure the electron density associated with the CO ligand can be described by a tube extending from the iron into the heme pocket over more than 4 A. This density can be interpreted by two discrete positions of the CO molecule. One is close to the heme iron and can be identified to be bound CO. In the second, the CO is dissociated from the heme iron and lies on top of pyrrole ri…

PhotonsBinding SitesPhotolysisMultidisciplinaryFourier AnalysisMyoglobinProtein ConformationLigandPhotodissociationWhalesHemeCrystallography X-Raychemistry.chemical_compoundCrystallographychemistryMetmyoglobinMyoglobinAnimalsMoleculeMetmyoglobinHemeResearch ArticlePyrroleCarbon monoxideProceedings of the National Academy of Sciences
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Myoglobin embedded in saccharide amorphous matrices: water-dependent domains evidenced by small angle X-ray scattering

2010

We report Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin (MbCO) embedded in low-water trehalose glasses. Results showed that, in such samples, "low-protein" trehalose-water domains are present, surrounded by a protein-trehalose-water background; such finding is supported by Infrared Spectroscopy (FTIR) measurements. These domains, which do not appear in the absence of the protein and in analogous sucrose systems, preferentially incorporate the incoming water at the onset of rehydration, and disappear following large hydration. This observation suggests that, in organisms under anhydrobiosis, analogous domains could play a buffering role against th…

Photosynthetic reaction centreSucroseGLASS-TRANSITIONGeneral Physics and AstronomyInfrared spectroscopyRhodobacter sphaeroideschemistry.chemical_compoundRhodobacter sphaeroidesScattering Small AngleSpectroscopy Fourier Transform InfraredPHOSPHOLIPID-BILAYERREACTION CENTERSPhysical and Theoretical ChemistrySettore CHIM/02 - Chimica FisicabiologyScatteringSmall-angle X-ray scatteringMyoglobinTrehaloseWaterbiology.organism_classificationPROTEIN DYNAMICSTrehaloseMOLECULAR-DYNAMICS SIMULATIONAmorphous solidCrystallographyMyoglobinchemistryTHERMAL-DENATURATIONNEUTRON-SCATTERINGCARBOXY-MYOGLOBINEXTERNAL MATRIXTREHALOSE-COATED MBCO
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