Search results for "Reaction intermediate"

showing 10 items of 35 documents

Electrochemical reduction and carboxylation of halobenzophenones

2002

Abstract The electrochemical reduction of a series of halogenated benzophenones XC6H4COC6H4Y (1) was studied in aprotic solvents, in the absence and presence of CO2, by cyclic voltammetry (CV) and controlled-potential electrolysis. The mechanism of electroreduction in dimethylformamide (DMF) has been investigated in some detail. Most of the compounds undergo reductive carbonhalogen bond cleavage in the time window of CV. The radical anions derived from difluorobenzophenones (X=Y=4-F; X=2-F, Y=4-F) as well as from the 3-chloro derivative are quite stable with a cleavage rate constant (kc) of the order of 10−2 s−1 or less. With 4-chloro-, 2-chloro-, 4,4′-dichloro- and 2,4′-dichorobenzophen…

ElectrolysishydroxyacidChemistryGeneral Chemical EngineeringInorganic chemistryElectrochemicalreductionReaction intermediateElectrochemistryAnalytical Chemistrylaw.inventioncarboxylationchemistry.chemical_compoundhalobenzophenoneReaction rate constantCarboxylationlawElectrochemistryDimethylformamideCyclic voltammetryBond cleavage
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Isolation of a Putative Hydroxyacyl Enzyme Intermediate of an Epoxide Hydrolase

1994

A putative covalent, alpha-hydroxyacyl intermediate was isolated by the brief exposure of murine soluble epoxide hydrolase to its substrate. The reaction was reversed by time and blocked by competitive inhibitors. The formation of the intermediate was dependent upon the concentration of the enzyme and was increased by incubation under acidic conditions. The structure of the intermediate was supported by microchemical methods.

Epoxide HydrolasesEpoxide hydrolase 2chemistry.chemical_classificationReaction mechanismStereochemistryAcylationBiophysicsSubstrate (chemistry)Cell BiologyReaction intermediateHydrogen-Ion ConcentrationTritiumBiochemistryRecombinant ProteinsKineticsMiceEnzymechemistryBiochemistryCovalent bondAnimalsHumansEpoxide hydrolaseMolecular BiologyIncubationBiochemical and Biophysical Research Communications
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The mechanism of formamide hydrolysis in water from ab initio calculations and simulations.

2005

The neutral hydrolysis of formamide in water is a suitable reference to quantify the efficiency of proteolytic enzymes. However, experimental data for this reaction has only very recently been obtained and the kinetic constant determined experimentally is significantly higher than that predicted by previous theoretical estimations. In this work, we have investigated in detail the possible mechanisms of this reaction. Several solvent models have been considered that represent a considerable improvement on those used in previous studies. Density functional and ab initio calculations have been carried out on a system which explicitly includes the first solvation shell of the formamide molecule…

FormamideModels MolecularReaction mechanismFormamidesMolecular StructureReaction stepHydrolysisOrganic ChemistryProteolytic enzymesHydrogen BondingGeneral ChemistryReaction intermediateCrystallography X-RayCatalysischemistry.chemical_compoundSolvation shellchemistrySolvent modelsAb initio quantum chemistry methodsComputational chemistryThermodynamicsComputer SimulationChemistry (Weinheim an der Bergstrasse, Germany)
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CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin

2013

Abstract: Cytoglobin (Cygb) was recently discovered in the human genome and localized in different tissues. It was suggested to play tissue-specific protective roles, spanning from scavenging of reactive oxygen species in neurons to supplying oxygen to enzymes in fibroblasts. To shed light on the functioning of such versatile machinery, we have studied the processes supporting transport of gaseous heme ligands in Cygb. Carbon monoxide rebinding shows a complex kinetic pattern with several distinct reaction intermediates, reflecting rebinding from temporary docking sites, second order recombination, and formation (and dissociation) of a bis-histidyl heme hexacoordinated reaction intermediate…

Genetics and Molecular Biology (all)ProteomicsProtein FoldingProtein ConformationMolecular biologylcsh:MedicineCrystallography X-RayLigandsBiophysics SimulationsBiochemistrychemistry.chemical_compoundProtein structureMacromolecular Structure AnalysisCinètica enzimàticaBinding Sites; Carbon Monoxide; Crystallography X-Ray; Globins; Humans; Kinetics; Ligands; Molecular Dynamics Simulation; Oxygenases; Point Mutation; Protein Binding; Protein Conformation; Medicine (all); Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)Biomacromolecule-Ligand Interactionslcsh:ScienceHemeCarbon MonoxideCrystallographyHemoproteinsMultidisciplinaryMedicine (all)PhysicsCytoglobinMetabolismeGlobinsBiochemistryOxygenasesddc:500Engineering sciences. TechnologyProtein BindingResearch ArticleBioquímicaProtein StructureBiophysicsReaction intermediateMolecular Dynamics SimulationProtein ChemistryGeneticsHumansPoint MutationGlobinProtein InteractionsBiologyBiologia molecularBinding SitesLigandCytoglobinlcsh:REnzyme kineticsOxygen transportProteinsComputational BiologyKineticsMetabolismAgricultural and Biological Sciences (all)chemistryX-RayBiophysicslcsh:QHuman medicineGenèticaCarbon monoxide
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Acetylation of 5-Amino-1H-[1,2,4]triazole Revisited

2002

The products of the acetylation reactions of the common herbicide 5-amino-1H-[1,2,4]triazole were investigated using HPLC, GC-MS, 1H NMR, and FTIR spectroscopy. The conventional annular monoacetylation procedures with acetyl chloride are not regioselective and furnish a mixture of isomers. Traditional diacetylation in neat acetic anhydride under reflux produces a mixture of di-, mono-, and triacetylated derivatives. By using equivalent amounts of acetic anhydride in a dimethylformamide solution, a rapid and selective annular monoacetylation of 5-amino-1H-[1,2,4]triazole was achieved. The monoacetylation proceeds via the formation of the intermediate, 1-acetyl-3-amino-1H-[1,2,4]triazole, whi…

Magnetic Resonance SpectroscopyChemistryStereochemistryTriazoleRegioselectivity124-TriazoleAcetylationGeneral ChemistryReaction intermediateMedicinal chemistryGas Chromatography-Mass Spectrometrychemistry.chemical_compoundAcetic anhydrideAcetyl chlorideSpectroscopy Fourier Transform InfraredDimethylformamideGeneral Agricultural and Biological SciencesSelectivityChromatography High Pressure LiquidAmitroleJournal of Agricultural and Food Chemistry
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Theoretical characterization of the photochemical reaction CO2 + O(3P) → CO + O2 related to experiments in solid krypton

2020

Abstract Formation and decomposition of the complex of carbon dioxide and atomic oxygen are characterized by quantum chemistry methods aiming to rationalize experimental studies in solid krypton. The observed FTIR spectra reflected the temporal evolution of the system after irradiation showing the bands of reactants, intermediates and products. Advanced quantum chemistry calculations show that the T-shape complex CO2…O(3P) can be formed in the matrix. Its excitation by the 193 nm light results in the charge-transfer state CO2+…O−, which evolves to the reaction intermediate CO3. The latter species decomposes to CO + O2 following pathways on the excited state energy surfaces.

Materials scienceKryptonMatrix isolationGeneral Physics and Astronomychemistry.chemical_element02 engineering and technologyReaction intermediate010402 general chemistry021001 nanoscience & nanotechnologyPhotochemistry01 natural sciencesDecompositionQuantum chemistry0104 chemical scienceschemistryExcited stateIrradiationPhysical and Theoretical Chemistry0210 nano-technologyExcitationChemical Physics Letters
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Unusual stability of reaction intermediates in ortho-metalation reactions of dicyclohexylphenylphosphane with dirhodium(II) tetraacetate

2013

Abstract Reaction of dirhodium(II) tetraacetate with 1 molar equivalent of dicyclohexylphenylphosphane afforded the complex [Rh 2 (μ-O 2 CCH 3 ) 3 {μ-(C 6 H 4 )PCy 2 }(CH 3 COOH) 2 ] ( 1 ) in which the phosphane ligand is coordinated to the rhodium atoms in a bridging ortho -metalated mode. As a second product, [Rh 2 (μ-O 2 CCH 3 ) 3 {μ-(C 6 H 4 )PCy 2 }(CH 3 COOH)(PhPCy 2 )] ( 2 ) was isolated from the same reaction. 2 proved to be unusually stable toward further reaction to a doubly ortho -metalated complex which has been accessible in the reaction of dirhodium(II) tetraacetate with other phosphane ligands. However, doubly ortho -metalated [Rh 2 (μ-O 2 CCH 3 ) 2 {μ-(C 6 H 4 )PCy 2 } 2 (CH…

MetalationStereochemistryLigandOrganic Chemistrychemistry.chemical_elementReaction intermediateCrystal structureBiochemistryRhodiumInorganic ChemistrychemistryMaterials ChemistryThermal reactionPhysical and Theoretical ChemistryJournal of Organometallic Chemistry
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Dehydrogenation versus Oxygenation in Two-Electron and Four-Electron Reduction of Dioxygen by 9-Alkyl-10-methyl-9,10-dihydroacridines Catalyzed by Mo…

2004

Dehydrogenation of 10-methyl-9,10-dihydroacridine (AcrH(2)) by dioxygen (O(2)) proceeds efficiently, accompanied by the two-electron and four-electron reduction of O(2) to produce H(2)O(2) and H(2)O, which are effectively catalyzed by monomeric cobalt porphyrins and cofacial dicobalt porphyrins in the presence of perchloric acid (HClO(4)) in acetonitrile (MeCN) and benzonitrile (PhCN), respectively. The cobalt porphyrin catalyzed two-electron reduction of O(2) also occurs efficiently by 9-alkyl-10-methyl-9,10-dihydroacridines (AcrHR; R = Me, Et, and CH(2)COOEt) to yield 9-alkyl-10-methylacridinium ion (AcrR+) and H(2)O(2). In the case of R = Bu(t) and CMe(2)COOMe, however, the catalytic two…

Metalloporphyrinschemistry.chemical_elementElectronsReaction intermediatePhotochemistryBiochemistryMedicinal chemistryCatalysisCatalysischemistry.chemical_compoundColloid and Surface ChemistryDehydrogenationPerchloric acidAlkylchemistry.chemical_classificationPerchloratesChemistryCobaltGeneral ChemistryNADPorphyrinKineticsBenzonitrileAcridinesHydrogenationOxidation-ReductionCobaltJournal of the American Chemical Society
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Modeling of the role of conformational dynamics in kinetics of the antigen-antibody interaction in heterogeneous phase.

2012

[EN] A novel approach that may potentially be used to study biomolecular interactions including the simultaneous determination of structural and kinetic binding parameters is described in this Article for the first time. It allows a rigid distinction between the possible reaction mechanisms of biomolecular recognition, induced fit and conformational selection. The relative importance of the two pathways is determined not by comparing rate constants but the structural aspects of the interaction instead. So the exact location of antigen molecules with respect to the capture antibody is depicted experimentally, avoiding the use of X-ray crystallography. The proposed pattern is applied to study…

Models MolecularTime FactorsSimultaneous determinationsProtein ConformationRate constantsBinding processAntigen-Antibody ComplexImmunoglobulin GFragment antigen-bindingConformational dynamicsMiceStructural aspectsBiomolecular recognitionMaterials ChemistrySteric hindrancesBovine serum albuminReaction mechanismbiologyChemistryIn-situSerum Albumin BovineLigand (biochemistry)Reaction schemesSurfaces Coatings and FilmsConformationsAntigen-antibody interactionBovine serum albuminsBiomolecular interactionsMolecular recognitionBSA moleculesAlgorithmsProtein BindingStereochemistryKinetic bindingReaction intermediateAntigen bindingAntibodiesMolecular recognitionAntigenQUIMICA ANALITICAAnimalsComputer SimulationPhysical and Theoretical ChemistryAntigensHeterogeneous phaseInduced fitX ray crystallographyMoleculesSensing surfaceKineticsSilicon chipInterferometryConformational selectionImmunoglobulin Gbiology.proteinBiophysicsCattleAntigen-antibody interactionThe journal of physical chemistry. B
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Conformational dynamics of active site loops 5, 6 and 7 of enzyme Triosephosphate Isomerase: A molecular dynamics study

2018

AbstractTriosephosphate Isomerase is a glycolytic enzyme catalyzing the interconversion of Dihydroxyacetone phosphate to Glyceraldehyde-3-phosphate. The active site is comprised of three distinct loops loop-6, loop-7 and loop-8. Based on loop-6 and loop-7 conformation we describe the enzyme as Open TIM and Closed TIM. Various NMR, X-ray crystallography and QM/MM simulation techniques have provided glimpses of individual events of what is essentially a dynamic process. We studied the conformational changes of two distinct loops (loop-6 and loop-7) enveloping the active site, in the presence of natural substrate, reaction intermediates and inhibitor molecules, by means of microsecond atomisti…

Molecular dynamicsCrystallographybiologyChemistrybiology.proteinSubstrate (chemistry)Active siteCrystal structureReaction intermediateDihedral angleLigand (biochemistry)Triosephosphate isomerase
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