Search results for " active site"

showing 4 items of 4 documents

Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Different relaxations in myoglobin after photolysis

2004

To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration in myoglobin (Mb), we measured time-resolved absorption spectra in the Soret region after photolysis of carbon monoxide Mb (MbCO) in the temperature interval 120-260 K and in the time window 350 ns to 200 ms. The spectral contributions of both photolyzed (Mb * ) and liganded Mb (MbCO) have been analyzed by taking into account homogeneous bandwidth, coupling to vibrational modes, and static conformational heterogeneity. We succeeded in separating the “time-dependent” spectral changes, and this work provides possibilities to identify the events in the process of ligand rebinding. KHB is domina…

Myoglobin Molecular Dynamics Simulation active siteAbsorption spectroscopyKineticsAnalytical chemistryThermodynamicsIn Vitro TechniquesKinetic energyLigandschemistry.chemical_compoundAnimalsMultidisciplinaryBinding SitesPhotolysisLigandMyoglobinPhotodissociationTemperatureWhalesBiological SciencesKineticsMyoglobinchemistrySpectrophotometryMolecular vibrationThermodynamicsCarbon monoxide
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Spectral broadening of the Soret band in myoglobin: an interpretation by the full spectrum of low-frequency modes from a normal modes analysis.

2005

In this work the temperature dependence of the Soret band line shape in carbon-monoxy myoglobin is re-analyzed by using both the full correlator approach in the time domain and the frequency domain approach. The new analyses exploit the full density of vibrational states of carbon-monoxy myoglobin available from normal modes analysis, and avoid the artificial division of the entire set of vibrational modes coupled to the Soret transition into "high-frequency" and "low-frequency" subsets; the frequency domain analysis, however, makes use of the so-called short-times approximation, while the time domain one avoids it. Time domain and frequency domain analyses give very similar results, thus s…

Myoglobin Molecular Dynamics Simulation active siteChemistryMyoglobinSpectrum AnalysisAnharmonicityBiophysicsAnalytical chemistryTemperatureGeneral MedicineMolecular physicsVibrationSpectral lineModels ChemicalNormal modeMolecular vibrationFrequency domainComputer SimulationTime domainHarmonic oscillatorDoppler broadeningEuropean biophysics journal : EBJ
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Multi-Alkenylsilsesquioxanes as Comonomers and Active Species Modifiers of Metallocene Catalyst in Copolymerization with Ethylene.

2018

The copolymers of ethylene (E) with open-caged iso-butyl-substituted tri-alkenyl-silsesquioxanes (POSS-6-3 and POSS-10-3) and phenyl-substituted tetra-alkenyl-silsesquioxane (POSS-10-4) were synthesized by copolymerization over the ansa-metallocene catalyst. The influence of the kind of silsesquioxane and of the copolymerization conditions on the reaction performance and on the properties of the copolymers was studied. In the case of copolymerization of E/POSS-6-3, the positive comonomer effect was observed, which was associated with the influence of POSS-6-3 on transformation of the bimetallic ion pair to the active catalytic species. Functionality of silsesquioxanes and polymerization par…

Polymers and Plastics02 engineering and technologyPost-metallocene catalyst010402 general chemistry01 natural sciencesArticlelcsh:QD241-441chemistry.chemical_compoundlcsh:Organic chemistryPolymer chemistryCopolymerethylenecrosslinkingchemistry.chemical_classificationmetalloceneComonomerGeneral ChemistryPolymer021001 nanoscience & nanotechnologySilsesquioxaneethylene; polyhedral oligomeric silsesquioxanes (POSS); copolymerization; metallocene; crosslinking; active site modifier0104 chemical sciencesactive site modifiercopolymerizationchemistryPolymerization0210 nano-technologyGlass transitionMetallocenepolyhedral oligomeric silsesquioxanes (POSS)Polymers
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