Search results for "PHOSPHATE"

showing 10 items of 1874 documents

Pyrophosphate-mediated magnetic interactions in Cu(II) coordination complexes.

2010

The reaction in water of Cu(NO(3))(2)·2.5H(2)O with 2,2'-bipyridine (bipy), 1,10-phenanthroline (phen), or 1,10-phenanthroline-5-amine (phenam), and sodium pyrophosphate (Na(4)P(2)O(7)), at various pHs, afforded three new copper(II)-pyrophosphate complexes, namely, {[Cu(bipy)(cis-H(2)P(2)O(7))](2)}·3H(2)O (1a), {[Cu(phen)(H(2)O)](4)(HP(2)O(7))(2)}(ClO(4))(2)·4H(2)O (2), and {[Cu(2)(phenam)(2)(P(2)O(7))](2)·25H(2)O}(n) (3). A solvent free crystalline phase of 1a was also isolated with formula {[Cu(bipy)(trans-H(2)P(2)O(7))](2)} (1b), which can be regarded as a pseudo-polymorph of 1a. Single crystal X-ray analyses revealed these compounds to have uncommon molecular architectures, with 3 being…

Models MolecularStereochemistryPolymersSodiumchemistry.chemical_elementCrystallography X-RayPyrophosphateInorganic Chemistrychemistry.chemical_compoundMagneticsStructure-Activity Relationship22'-DipyridylCoordination ComplexesMoleculePhysical and Theoretical ChemistryMathematical ComputingSolvent freeMolecular StructureCationic polymerizationHydrogen-Ion ConcentrationCopperDiphosphatesCrystallographychemistryThermodynamicsSingle crystalDimerizationCopperPhenanthrolinesInorganic chemistry
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Toward very potent, non-covalent organophosphonate inhibitors of cathepsin C and related enzymes by 2-amino-1-hydroxy-alkanephosphonates dipeptides

2013

Cathepsins play an important role in several human disorders and therefore the design and synthesis of their inhibitors attracts considerable interest in current medicinal chemistry approaches. Due to the presence of a strong sulphydryl nucleophile in the active center of the cysteine type cathepsins, most strategies to date have yielded covalent inhibitors. Here we present a series of non-covalent β-amino-α-hydroxyalkanephosphonate dipeptidic inhibitors of cathepsin C, ranking amongst the best low-molecular weight inhibitors of this enzyme. Their binding modes determined by molecular modelling indicate that the hydroxymethyl fragment of the molecule, not the phosphonate moiety, acts as a t…

Models MolecularStereochemistryhydroxyphosphonateBiochemistryCathepsin CCathepsin BCathepsin CInhibitory Concentration 50chemistry.chemical_compoundCathepsin OTransition state analogCathepsin KHumanscysteine proteasePeptide bondcathepsinAminesEnzyme InhibitorsCathepsinDipeptideChemistryMolecular MimicryDipeptidesGeneral MedicineOrganophosphatesEnzyme ActivationinhibitorBiochemistryHydroxy AcidsBiochimie
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Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor

2020

The P2X7 receptor (P2X7R) possesses a unique structure associated to an as yet not fully understood mechanism of action that facilitates cell permeability to large ionic molecules through the receptor itself and/or nearby membrane proteins. High extracellular adenosine triphosphate (ATP) levels—inexistent in physiological conditions—are required for the receptor to be triggered and contribute to its role in cell damage signaling. The inconsistent data on its activation pathways and the few studies performed in natively expressed human P2X7R have led us to review the structure, activation pathways, and specific cellular location of P2X7R in order to analyze its biological relevance. The ATP-…

Models MolecularTranscription GeneticP2X7 receptor physiological rolechannel membrane proteinsAllosteric regulationReviewModels BiologicalCatalysislcsh:ChemistryInorganic ChemistryTransduction (genetics)chemistry.chemical_compoundAdenosine Triphosphateallosteric modulationsmedicineExtracellularAnimalsHumansPhysical and Theoretical ChemistryProtein Structure QuaternaryReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyhuman P2X7 receptor isoformsPolymorphism GeneticCell MembraneOrganic ChemistryGeneral MedicineComputer Science ApplicationsCell biologyATPlcsh:Biology (General)lcsh:QD1-999Mechanism of actionchemistryMembrane proteinP2X7 receptorReceptors Purinergic P2X7medicine.symptomAdenosine triphosphateIntracellularSignal TransductionInternational Journal of Molecular Sciences
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8-N(3)-3'-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue.

2001

A novel photoaffinity label, 8-N(3)-3'-biotinyl-ATP, has been synthesized. The introduction of an additional biotin residue is advantageous for easy detection of labeled proteins. This could be first tested by reaction with the F(1)-ATPase from the thermophilic bacterium PS3 (TF(1)). UV irradiation of TF(1) in the presence of 8-N(3)-3'-biotinyl-ATP results in a nucleotide-dependent binding of the analogue in the noncatalytic alpha and the catalytic beta subunits of TF(1), demonstrating the suitability of this analogue as a potential photoaffinity label. Reaction with the V(1)-ATPase, however, led to labeling of subunit E, which has been suggested as a structural and functional homologue of …

Models MolecularVacuolar Proton-Translocating ATPasesTime FactorsUltraviolet RaysProtein subunitATPaseBiophysicsCoated vesicleBiotinPhotoaffinity LabelsPhotoaffinity LabelsBiochemistryCatalysischemistry.chemical_compoundAdenosine TriphosphateBiotinBacterial ProteinsManducaAnimalsBinding siteMolecular BiologyBinding SitesPhotoaffinity labelingbiologyChemistryCell BiologyProton-Translocating ATPasesBiochemistryModels ChemicalSpectrophotometrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinCattleGamma subunitProtein BindingBiochemical and biophysical research communications
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Structural and functional consequences of the replacement of proximal residues Cys172 and Cys192 in the large subunit of ribulose-1,5-bisphosphate ca…

2008

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect of the replacement of Cys(172) and Cys(192) by serine on the catalytic properties, thermostability and three-dimensional structure of Chlamydomonas reinhardtii Rubisco. The most striking effect of the C172S substitution was an 11% increase in the specificity factor when compared wi…

Models Molecularinorganic chemicalsOxygenaseRibulose-Bisphosphate CarboxylaseProtein subunitSpecificity factorChlamydomonas reinhardtiiCrystallography X-RayBiochemistryCatalysischemistry.chemical_compoundEnzyme StabilityAnimalsCysteineMolecular BiologyBinding SitesRibulose 15-bisphosphatebiologyfungiRuBisCOTemperaturefood and beveragesCell Biologybiology.organism_classificationLyaseMolecular biologyProtein Structure TertiaryPyruvate carboxylaseKineticsProtein SubunitsBiochemistrychemistryMutationbiology.proteinChlamydomonas reinhardtiiBiochemical Journal
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Multiple Decay Mechanisms and 2D-UV Spectroscopic Fingerprints of Singlet Excited Solvated Adenine-Uracil Monophosphate

2016

The decay channels of singlet excited adenine uracil monophosphate (ApU) in water are studied with CASPT2//CASSCF:MM potential energy calculations and simulation of the 2D-UV spectroscopic fingerprints with the aim of elucidating the role of the different electronic states of the stacked conformer in the excited state dynamics. The adenine 1La state can decay without a barrier to a conical intersection with the ground state. In contrast, the adenine 1Lb and uracil S(U) states have minima that are separated from the intersections by sizeable barriers. Depending on the backbone conformation, the CT state can undergo inter-base hydrogen transfer and decay to the ground state through a conical …

Models Molecularmolecular electronicsChemistry MultidisciplinaryMolecular electronicsphotophysic2-DIMENSIONAL ELECTRONIC SPECTROSCOPYSTATE DYNAMICSBASE-STACKINGPhotochemistry01 natural sciences[CHIM] Chemical SciencesNUCLEIC-ACIDSQuímica quànticaEspectrofotometriaConformational isomerismComputingMilieux_MISCELLANEOUSphotophysics010304 chemical physicsFull PaperHydrogen bondChemistryChemistry (all)Full PapersMolecular spectroscopy[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryChemistryFOURIER-TRANSFORM SPECTROSCOPYSpectrophotometryExcited statePhysical Sciences1ST-PRINCIPLES SIMULATION03 Chemical SciencesGround stateUridine MonophosphateQuantum chemistryEspectroscòpia molecularmolecular electronic010402 general chemistryMolecular physicsCatalysisUltraviolet visible spectroscopy0103 physical sciencesPhotophysics | Hot Paper[CHIM]Chemical SciencesSinglet stateUV/Vis spectroscopyULTRAFAST INTERNAL-CONVERSIONSpectroscopyLIGHT-HARVESTING COMPLEXab initio calculationScience & Technologyab initio calculationsOrganic ChemistryGeneral ChemistryDNAConical intersectionDNA FingerprintingAdenosine Monophosphate0104 chemical sciences[CHIM.THEO] Chemical Sciences/Theoretical and/or physical chemistryAB-INITIO SIMULATIONSElectrònica molecularMOLECULAR-DYNAMICSSpectrophotometry Ultraviolet
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Dynamical Properties of Self-Assembled Surfactant-Based Mixtures: Triggering of One-Dimensional Anomalous Diffusion in Bis(2-ethylhexyl)phosphoric Ac…

2013

The dynamic features of bis(2-ethylhexyl)phosphoric acid (HDEHP)/n-octylamine (NOA) mixtures have been investigated as a function of the NOA mole fraction and temperature by (1)H NMR spectroscopy and rheometry. All data consistently suggest a composition-induced glass-forming behavior. The microscopic factors responsible for this behavior have been highlighted and have been explained in terms of driving forces given by HDEHP-to-NOA proton transfer, the tendency of the resulting species to establish H bonds and to spatially segregate the alkyl chains. The study sheds light on the molecular mechanism responsible for the peculiar behavior of transport properties in such systems and furnishes b…

Models Molecularsurfactant mixtures self-assembly dynamical propertiesProtonAnomalous diffusionMole fractionSelf assembledDiffusionSurface-Active Agentschemistry.chemical_compoundPulmonary surfactantElectrochemistryOrganic chemistryGeneral Materials ScienceAminesPhosphoric acidSpectroscopyAlkylSettore CHIM/02 - Chimica Fisicachemistry.chemical_classificationMolecular StructureRheometryChemistrySurfaces and InterfacesCondensed Matter PhysicsOrganophosphatesThermodynamicsPhysical chemistryRheologyLangmuir
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Reduction of Polymerization Shrinkage Stress and Marginal Microleakage Using Soft-Start Polymerization

2003

Purpose: This study evaluated the influence of a soft-start light-curing exposure on polymerization shrinkage stress and marginal integrity of adhesive restorations. Materials and Methods: Six resin-based composites (Pertac II, Tetric Ceram, Definite, Surefil, Solitaire, and Visio-Molar) were adhesively bonded to a cylindrical cavity (n = 9 per material/light) in a photoelastic material. Visible light-curing was applied using either the standard polymerization mode (800 mW/cm2 exposure duration 40 s) of the curing light (Elipar TriLight, 3M ESPE) or the exponential mode from the same device (ramp-curing: 150 mW/cm2 to 800 mW/cm2 within the first 15 s of a total curing time of 40 s). Polymer…

MolarTime FactorsMaterials scienceSiloxanesPolymersSurface PropertiesComposite ResinsPhosphatesAcetonePolymethacrylic AcidsHardnessMaterials TestingHumansBisphenol A-Glycidyl MethacrylatePhosphoric AcidsComposite materialDental EnamelGeneral DentistryLightingCuring (chemistry)ShrinkageDental CementumDental LeakageEthanolEnamel paintTerpenesQuartzDental Marginal AdaptationHardnessDental Marginal AdaptationResin CementsPolymerizationDentin-Bonding Agentsvisual_artvisual_art.visual_art_mediumMethacrylatesAdhesiveJournal of Esthetic and Restorative Dentistry
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Mapping of a binding site for ATP within the extracellular region of the Torpedo nicotinic acetylcholine receptor beta-subunit.

1997

Using 2,8,5'-[H-3]ATP as a direct photoaffinity label for membrane-bound nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata, we have identified a binding site for ATP in the extracellular region of the beta-subunit of the receptor. Photolabeling was completely inhibited in the presence of saturating concentrations of nonradioactive ATP, whereas neither the purinoreceptor antagonists suramin, theophyllin, and caffeine nor the nAChR antagonists alpha-bungarotoxin and d-tubocurarine affected the labeling reaction. Competitive and noncompetitive nicotinic agonists and Ca2+ increased the yield of the photoreaction by up to 50%, suggesting that the respective binding sites are allost…

Molecular Sequence DataPhotoaffinity LabelsReceptors NicotinicTorpedoTritiumBiochemistryPeptide Mappingchemistry.chemical_compoundGanglion type nicotinic receptorAdenosine TriphosphateAdenine nucleotideAnimalsChymotrypsinTrypsinAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisCell MembranePeptide FragmentsNicotinic acetylcholine receptorNicotinic agonistBiochemistrychemistrybiology.proteinAlpha-4 beta-2 nicotinic receptorExtracellular SpaceAdenosine triphosphateSequence AnalysisATP synthase alpha/beta subunitsBiochemistry
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