Search results for "Oxygen binding"

showing 10 items of 48 documents

Entrapment and characterization of functional allosteric conformers of hemocyanin in sol–gel matrices

2016

Hemocyanins are giant oxygen transport proteins of molluscs and arthropods, which display high cooperativity and a complex pattern of conformations, generated by hierarchical allosteric interactions of their complex quaternary structure. A still unanswered question is the correlation between the functional properties of the postulated conformers and structural features that govern their oxygen binding, such as metal complex coordination. In this study we focus on the dodecameric hemocyanin of the crustacean Carcinus aestuarii, with the aim to obtain a functional and structural characterization of the individual conformational states giving rise to cooperativity, by entrapping hemocyanin int…

0301 basic medicinebiologyChemistryGeneral Chemical Engineeringmedicine.medical_treatmentOxygen transportActive siteCooperativityHemocyaninGeneral ChemistryProtein structure allosteric regulation hemocyaninallosteric regulation03 medical and health sciencesCrystallography030104 developmental biologyProtein structurebiology.proteinmedicineProtein quaternary structurehemocyaninConformational isomerismOxygen bindingMacromoleculeRSC Advances
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Oxygen binding properties of non-mammalian nerve globins

2006

Oxygen-binding globins occur in the nervous systems of both invertebrates and vertebrates. While the function of invertebrate nerve haemoglobins as oxygen stores that extend neural excitability under hypoxia has been convincingly demonstrated, the physiological role of vertebrate neuroglobins is less well understood. Here we provide a detailed analysis of the oxygenation characteristics of nerve haemoglobins from an annelid (Aphrodite aculeata), a nemertean (Cerebratulus lacteus) and a bivalve (Spisula solidissima) and of neuroglobin from zebrafish (Danio rerio). The functional differences have been related to haem coordination: the haem is pentacoordinate (as in human haemoglobin and myogl…

AnnelidaDanioNeuroglobinNerve Tissue ProteinsCooperativityBiochemistryHemoglobinschemistry.chemical_compoundJournal ArticleAnimalsGlobinNerve TissueMolecular BiologyConserved SequenceZebrafishAnnelidbiologyResearch Support Non-U.S. Gov'tTemperatureHexacoordinateCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationGlobinsOxygenMyoglobinchemistryBiochemistryNeuroglobinOxygen binding
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Nested allosteric interactions in extracellular hemoglobin of the leech Macrobdella decora

2003

Hemoglobin from the leech Macrobdella decora belongs to the class of giant extracellular hexagonal bilayer globin structures found in annelid and vestimentiferan worms. These complexes consist of 144 heme-bearing subunits, exhibit a characteristic quaternary structure (2 × (6 × (3 × 4))), and contain tetramers as basic substructures that express cooperative oxygen binding and thus provide a structural basis for a hierarchy in allosteric interactions. A thorough analysis of the isolated tetramer indicates that it functions as a trimer of cooperatively interacting subunits and a non-cooperative monomer rather than as four interacting subunits. A thermodynamic analysis of the whole molecule fa…

Binding Sitesgenetic structuresStereochemistryMacromolecular SubstancesProtein ConformationBilayerAllosteric regulationTrimerCell BiologyBiologyBiochemistryGroELOxygenHemoglobinsProtein SubunitsTetramerLeechesAnimalsProtein quaternary structureGlobinProtein Structure QuaternaryMolecular BiologyOxygen binding
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Exceptional affinity of nanostructured organic-inorganic hybrid materials towards dioxygen: confinement effect of copper complexes

2007

We report the exceptional reactivity towards dioxygen of a nanostructured organic-inorganic hybrid material due to the confinement of copper cyclam within a silica matrix. The key step is the metalation reaction of the ligand, which can occur before or after xerogel formation through the sol-gel process. The incorporation of a Cu(II) center into the material after xerogel formation leads to a bridged Cu(I)/Cu(II) mixed-valence dinuclear species. This complex exhibits a very high affinity towards dioxygen, attributable to auto-organization of the active species in the solid. The remarkable properties of these copper complexes in the silica matrix demonstrate a high cooperative effect for O(2…

Cations DivalentMetalationInorganic chemistrychemistry.chemical_elementLigands010402 general chemistry01 natural sciencesCatalysischemistry.chemical_compoundAdsorptionHeterocyclic CompoundsCyclamPolymer chemistryOrganometallic CompoundsLamellar structureReactivity (chemistry)ComputingMilieux_MISCELLANEOUSdioxygen bindingBinding Sites010405 organic chemistryLigandsol-gel processesSpectrum AnalysisOrganic ChemistryTemperatureGeneral Chemistry[CHIM.MATE]Chemical Sciences/Material chemistrySilicon DioxideCopperEnzymesNanostructuresPeroxides0104 chemical sciencesOxygenchemistrytetraazamacrocyclesMultiprotein Complexescopper[ CHIM.MATE ] Chemical Sciences/Material chemistryAnisotropyAdsorptionHybrid materialGelsorganic-inorganic hybrid composites
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Neuron-specific expression of neuroglobin in mammals.

2004

Neuroglobin, a vertebrate oxygen-binding protein, is expressed in many regions of the adult brain. We examined the cell type-specific expression of neuroglobin in neurons and astroglial cells in primary cultures of fetal hippocampal cells and sections of the adult mouse brain using neuroglobin-specific polyclonal antibodies and cell type-specific markers NeuN and GFAP to differentiate between neurons and glial cells. Neuroglobin is exclusively expressed in neurons, but not in astroglial cells. Accordingly, neuroglobin was detected in two neuroblastoma cell lines (N2a, SH-SY5Y) and the pheochromocytoma cell line PC-12, but not in glioblastoma cell lines (DKMG, GAMG) or other, non-neural cell…

CellNeuroglobinNerve Tissue ProteinsHippocampal formationRats Sprague-DawleyMiceCell Line TumorChlorocebus aethiopsmedicineAnimalsHumansGlobinVero CellsCells CulturedNeuronsMice Inbred BALB CbiologyGeneral NeuroscienceBrainMolecular biologyImmunohistochemistryGlobinsRatsmedicine.anatomical_structurenervous systemGene Expression RegulationMicroscopy FluorescenceNeuroglobinbiology.proteinNeurogliaNeuronNeuNOxygen bindingNeuroscience letters
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Molecular heterogeneity of the hemocyanin isolated from the king crabParalithodes camtschaticae

2000

Native Paralithodes camtschaticae hemocyanin is found as a mixture of dodecamers (24S; 80%) and hexamers (16S; 20%). Removal of Ca2+ ions by dialysis against EDTA-containing buffer solution at neutral pH induces complete dissociation of the 24S form into the 16S form. Under these conditions, a further increase in pH to 9.2 produces complete dissociation of the hexamers into monomers (5S). In both cases, the dissociation process is reversible. The dodecamer (24S) is composed of two different hexamers which can be discriminated only by ion-exchange chromatography in the presence of Ca2+ ions. At alkaline pH and in the presence of EDTA, two major monomeric fractions can be separated by ion-exc…

Chromatographymedicine.medical_treatmentHemocyaninBohr effectBuffer solutionBiochemistryDissociation (chemistry)Crystallographychemistry.chemical_compoundDodecameric proteinMonomerchemistrymedicineProtein quaternary structureOxygen bindingEuropean Journal of Biochemistry
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Control of kinetics by cooperative interactions.

2011

Cooperative effects in ligand binding and dissociation kinetics are much less investigated than steady state kinetics or equilibrium binding. Nevertheless, cooperativity in ligand binding leads necessarily to characteristic properties with respect to kinetic properties of the system. In case of positive cooperativity as found in oxygen binding proteins, a typical property is an autocatalytic ligand dissociation behavior leading to a time dependent, apparent ligand dissociation rate. To follow systematically the influence of the various potentially involved parameters on this characteristic property, simulations based on the simple MWC model were performed which should be relevant for all ty…

Clinical BiochemistryAllosteric regulationCooperative bindingThermodynamicsProteinsCooperativityCell BiologyLigand (biochemistry)LigandsBiochemistryDissociation (chemistry)Crystallographychemistry.chemical_compoundKineticschemistryAllosteric RegulationModels ChemicalGeneticsCharacteristic propertyMolecular BiologyOxygen bindingEquilibrium constantProtein BindingIUBMB life
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The Allosteric Effector l-Lactate Induces a Conformational Change of 2×6-meric Lobster Hemocyanin in the Oxy State as Revealed by Small Angle X-ray S…

2001

Abstract Hemocyanins are multisubunit respiratory proteins found in many invertebrates. They bind oxygen highly cooperatively. However, not much is known about the structural basis of this behavior. We studied the influence of the physiological allosteric effectorl-lactate on the oxygenated quaternary structure of the 2×6-meric hemocyanin from the lobster Homarus americanus employing small angle x-ray scattering (SAXS). The presence of 20 mm l-lactate resulted in different scattering curves compared with those obtained in the absence of l-lactate. The distance distribution functionsp(r) indicated a more compact molecule in presence ofl-lactate, which is also reflected in a reduction of the …

Conformational changeProtein ConformationScatteringChemistrySmall-angle X-ray scatteringmedicine.medical_treatmentAllosteric regulationHemocyaninCell BiologyBiochemistryNephropidaeMicroscopy ElectronCrystallographyAllosteric RegulationHemocyaninsRadius of gyrationmedicineAnimalsScattering RadiationProtein quaternary structureLactic AcidMolecular BiologyOxygen bindingJournal of Biological Chemistry
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Cascade complex formation by phosphate in the cobalt(II)/[30]aneN10 anaerobic system

1993

Abstract The interaction of phosphate with the mono- and binuclear cobalt(II) complexes of [30]aneN 10 (1,4,7,10,13,16,19,22,25,28-decaazacyclotriacontane) has been studied by potentiometry in 0.15 mol dm −3 NaClO 4 solution at 298.15 K under anaerobic conditions. The stable species [CoH 2 ([30]aneN 10 )PO 4 ] + , [CoH 4 ([30]aneN 10 )PO 4 ] 3+ , [Co 2 H([30]aneN 10 )PO 4 ] 2+ , [Co 2 H 2 ([30]aneN 10 )PO 4 ] 3+ and [Co 2 H 3 ([30]aneN 10 )PO 4 ] 4+ , where the phosphate anion is directly bound to the metal ions or acts as a second sphere ligand, are formed and their stability constants have been determined. The results obtained allowed for the selection of suitable conditions for the study…

DIOXYGEN CARRIERS; DIOXYGEN BINDING; Co(II) COMPLEXES; POLYAMINE LIGANDS; DITOPIC POLYAMINES; OPEN-CHAIN POLYAZAALKANES; THERMODYNAMICS; ANION COORDINATION CHEMISTRY; INCLUSION COMPLEXESINCLUSION COMPLEXESMetal ions in aqueous solutionComplex formationInorganic chemistryDIOXYGEN BINDINGchemistry.chemical_elementMedicinal chemistryCo(II) COMPLEXESInorganic Chemistrychemistry.chemical_compoundOPEN-CHAIN POLYAZAALKANESANION COORDINATION CHEMISTRYTHERMODYNAMICSMaterials ChemistryDIOXYGEN CARRIERSPhysical and Theoretical ChemistryLigandPhosphatePhosphate anionchemistryDITOPIC POLYAMINESChemical equilibriumAnaerobic exerciseCobaltPOLYAMINE LIGANDS
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A respiratory hemocyanin from an insect.

2004

Insects possess an elaborate tracheal system that enables transport of gaseous oxygen from the atmosphere directly to the inner organs. Therefore, the presence of specialized oxygen-transport proteins in the circulatory system of insects has been considered generally unnecessary. Here, we show for the first time, to our knowledge, the presence of an ancestral and functional hemocyanin (Hc) in an insect. In the hemolymph of nymphs and adults of the stonefly Perla marginata , a hexameric Hc was identified, which consists of two distinct subunit types of 659 and 655 amino acids. P. marginata Hc displays cooperative oxygen binding with a moderately high oxygen affinity [(half-saturation pressu…

DNA ComplementaryInsectamedicine.medical_treatmentProtein subunitmedia_common.quotation_subjectMolecular Sequence DataInsectBiologyEvolution MolecularCrustaceaHemolymphHemolymphmedicineAnimalsAmino Acid SequenceCloning MolecularNymphPhylogenymedia_commonchemistry.chemical_classificationMultidisciplinaryBase SequenceSequence Homology Amino AcidRespirationHemocyaninBiological SciencesAmino acidRespiratory proteinOxygenProtein SubunitschemistryBiochemistryHemocyaninsInsect ProteinsFemaleOxygen bindingProceedings of the National Academy of Sciences of the United States of America
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