Search results for "Dioxygen"

showing 10 items of 80 documents

Triggering the generation of an iron(IV)-oxo compound and its reactivity toward sulfides by RuII photocatalysis

2014

The preparation of [FeIV(O)(MePy2tacn)]2+ (2, MePy2tacn = N-methyl-N,N-bis(2-picolyl)-1,4,7-triazacyclononane) by reaction of [FeII(MePy2tacn)(solvent)]2+ (1) and PhIO in CH3CN and its full characterization are described. This compound can also be prepared photochemically from its iron(II) precursor by irradiation at 447 nm in the presence of catalytic amounts of [Ru II(bpy)3]2+ as photosensitizer and a sacrificial electron acceptor (Na2S2O8). Remarkably, the rate of the reaction of the photochemically prepared compound 2 toward sulfides increases 150-fold under irradiation, and 2 is partially regenerated after the sulfide has been consumed; hence, the process can be repeated several times.…

SulfideFotocatàlisi010402 general chemistryPhotochemistry01 natural sciencesBiochemistryChemical reactionArticleCatalysisCatalysisReaccions químiquesReaction rateColloid and Surface ChemistrySofre -- CompostosChemical reactionsSulphur compoundsOrganic chemistryWATER[CHIM.COOR]Chemical Sciences/Coordination chemistryPhotosensitizerReactivity (chemistry)Photocatalysischemistry.chemical_classificationOXYGENATION REACTIONS010405 organic chemistryChemistryGeneral ChemistryElectron acceptorSTATE0104 chemical sciencesELECTRON-TRANSFER PROPERTIESC-H OXIDATIONSPIN FE(IV) COMPLEXPhotocatalysisIRON-OXO COMPLEXESLIGANDTAURINE/ALPHA-KETOGLUTARATE DIOXYGENASENONHEME OXOIRON(IV) COMPLEXES
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Recruitment of HIF-1α and HIF-2α to common target genes is differentially regulated in neuroblastoma: HIF-2α promotes an aggressive phenotype

2006

In neuroblastoma specimens, HIF-2alpha but not HIF-1alpha is strongly expressed in well-vascularized areas. In vitro, HIF-2alpha protein was stabilized at 5% O2 (resembling end capillary oxygen conditions) and, in contrast to the low HIF-1alpha activity at this oxygen level, actively transcribed genes like VEGF. Under hypoxia (1% O2), HIF-1alpha was transiently stabilized and primarily mediated acute responses, whereas HIF-2alpha protein gradually accumulated and governed prolonged hypoxic gene activation. Knockdown of HIF-2alpha reduced growth of neuroblastoma tumors in athymic mice. Furthermore, high HIF-2alpha protein levels were correlated with advanced clinical stage and high VEGF expr…

Transcriptional ActivationCancer ResearchProcollagen-Proline DioxygenaseAggressive phenotypeCELLCYCLEBiologyMiceNeuroblastomaNeuroblastomaBasic Helix-Loop-Helix Transcription FactorsTumor Cells CulturedmedicineAnimalsHumansRNA MessengerChildHypoxiaGeneOligonucleotide Array Sequence AnalysisRegulation of gene expressionGene knockdownGene Expression ProfilingCell BiologyCell cycleHypoxia (medical)Hypoxia-Inducible Factor 1 alpha Subunitmedicine.diseaseIn vitroGene Expression Regulation NeoplasticOxygenPhenotypeOncologyImmunologyCancer researchFemalemedicine.symptomNeoplasm TransplantationCancer Cell
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Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia

2012

The function and survival of eukaryotic cells depends on a constant and sufficient oxygen supply. Cells recognize and respond to hypoxia by accumulation of the transcription factor hypoxia-inducible factor 1 (HIF-1), composed of an oxygen-sensitive HIF-1α and a constitutive HIF-1β subunit. Besides physiology, HIF-1 induction is involved in major pathological processes such as cardiovascular disease, inflammation and cancer, which are associated with the formation of reactive oxygen species (ROS). ROS have been reported to affect HIF-1 activity but the role for ROS in regulating HIF-1 has not been definitely settled. In order to shed light on the redox-regulation of HIF-1 by ROS, we studied …

Transcriptional ActivationProcollagen-Proline DioxygenaseMedizinBiologyTransfectionBiochemistryHypoxia-Inducible Factor-Proline DioxygenasesTransactivationCell Line TumormedicineHumansRNA Small InterferingTranscription factorchemistry.chemical_classificationRegulation of gene expressionReactive oxygen speciesGene knockdownGeneral MedicineTransfectionHydrogen PeroxideHypoxia (medical)Cell HypoxiaCell biologyHypoxia-inducible factorschemistryBiochemistryHypoxia-Inducible Factor 1medicine.symptomReactive Oxygen SpeciesOxidation-Reduction
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Production of a Recombinant Catechol 2,3-Dioxygenase for the Degradation of Micropollutants

2017

Phenolic compounds such as catechol represent a particular type of micropollutant whose high stability prevents rapid decay and metabolization in the environment. We successfully cloned a catechol 2,3-dioxygenase (C2,3O) from Pseudomonas putida mt-2 and expressed it in Escherichia coli BER2566. The biomass isolated from shake-flask fermentations was used to partially purify the enzyme. The enzyme proved unstable in clarified liquid fractions (50 mM Tris buffer, pH 7.6) and lost more than 90% of its activity over 7 h at 25 °C. In the presence of 10% acetone, the process was slowed down and 30% residual activity was still present after 7 h incubation. Storage of the enzyme in clear liquid fr…

TrisCatecholChromatographybiology010401 analytical chemistry02 engineering and technologyGeneral MedicineGeneral Chemistry021001 nanoscience & nanotechnologyAscorbic acidbiology.organism_classification01 natural sciencesPseudomonas putida0104 chemical scienceschemistry.chemical_compoundBiotransformationchemistryDioxygenaseAcetone0210 nano-technologyIncubationCHIMIA
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A Study Using X-ray Absorption and Emission Spectroscopy of Dioxygen-Binding Xerogels Incorporating Cyclam Units Complexed with Copper Salts.

2005

X-ray absorption spectroscopy was used to elucidate how hybrid xerogels complexed with CuCl2 could reversibly bind molecular dioxygen. Difference EXAFS analyses at the Cu K-edge suggest that dioxygen could bridge two Cu atoms in a μ-η1:η1 peroxo-like conformation with unequal Cu···O distances. Only the short distance (RCu–O1 = 1.86 ± 0.01 A) was unambiguously determined and looks typical of a CuII site. The Cu···Cu internuclear distances would be rather long: RCu–Cu ≈ 4.0 A (3.9 A) for the oxygenated (oxygen-free) xerogels. Cl K-edge EXAFS spectra revealed the pre-existence in the oxygen-free xerogels of CuI sites with short Cl–Cu bonds (2.11 ± 0.03 A). Pentacoordinate CuII sites with a lon…

[PHYS]Physics [physics]X-ray absorption spectroscopy[ PHYS ] Physics [physics]Absorption spectroscopyExtended X-ray absorption fine structure010405 organic chemistryAb initio010402 general chemistryResonance (chemistry)Photochemistry01 natural sciencesXANES0104 chemical sciencesInorganic Chemistrychemistry.chemical_compoundCrystallographychemistryCyclamAbsorption (chemistry)X-ray absorption spectroscopy • Tetraazamacrocyclic ligand • Dioxygen binding • Peroxo ligand • Copper
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Isoproturon

2010

Frequent use of phenylurea herbicide isoproturon (IPU) in agricultural fields has resulted not only in the contamination of the natural resources including soil and water but also in the adaptation of the soil microflora to its rapid degradation. However, up to now, the mechanisms underlying this microbial adaptation are not well elucidated. The aim of this study was to explore the processes and factors implicated in IPU degradation from the agricultural field to the genes coding for catabolic genes. The study carried out at the experimental field of Epoisses cropped with a winter wheat / barley / rape seed crop rotation indicated that as a result of its periodically repeated use, the soil …

[SDE] Environmental Sciences[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesHerbicidesVARIABILITE SPATIALE1Clonage BACSpatial variability[SDV] Life Sciences [q-bio]BAC cloningVOIE METABOLIQUESoil microbiologyMicrobiologie du sol12-DIOXYGENASEMetabolic pathwayBiodegradationVoie métaboliqueHerbicideIsoproturon2-dioxygenaseVariabilité spatiale
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Genomic approach to search for IPU degrading gene: catA as a possible gene target responsible for 4- isopropyl aniline degradation

2009

Affiche, résumé étendu; Genomic approach to search for IPU degrading gene: catA as a possible gene target responsible for 4- isopropyl aniline degradation

[SDV] Life Sciences [q-bio][ SDV ] Life Sciences [q-bio]bacterial consortiumphenylurea herbicideisoproturon[SDV]Life Sciences [q-bio]mineralizationisoproturon;bacterial consortium;mineralization;phenylurea herbicide;BAC library;dioxygenase genedioxygenase geneBAC library
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Use of PCAH as a molecular marker for estimating the diversity of the protocatechuate-degrading bacterial community in soil environment

2007

Microorganisms degrading phenolic compounds play an important role in soil carbon cycling. The pcaH gene encoding a key ring-cleaving enzyme of the β -ketoadipate pathway was selected as a functional marker. Using a degenerate primer pair, pcaH fragments were cloned from two soils. The RFLP screening of 150 pcaH clones yielded 68 RFLP families. Comparison of 86 deduced amino acid sequences displayed 70 % identity to known PcaH sequences. Phylogenetic analysis results in two major groups mainly related to PcaH sequences from Actinobacteria and Proteobacteria phyla. This gene constitutes a suitable molecular marker to study the diversity of this functional group.

[SDV] Life Sciences [q-bio][SDE] Environmental SciencesPROTOCATECHUATE[SDV]Life Sciences [q-bio]34-DIOXYGENASE[SDE]Environmental SciencesBACTERIAL COMMUNITYOIL DNA
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Regulatory changes in pterin and carotenoid genes underlie balanced color polymorphisms in the wall lizard

2019

Significance Reptiles show an amazing color diversity based on variation in melanins, carotenoids, and pterins. This study reveals genes controlling differences between three color morphs (white, orange, and yellow) in the common wall lizard. Orange pigmentation, due to high levels of orange/red pterins in skin, is caused by genetic changes in the sepiapterin reductase gene. Yellow skin, showing high levels of yellow carotenoids, is controlled by the beta-carotene oxygenase 2 locus. Thus, the color polymorphism in the common wall lizard is associated with changes in two small regions of the genome containing genes with crucial roles in pterin and carotenoid metabolism. These genes are likel…

balanced polymorphismBalanced polymorphismgenetic structuresEvolutionIntrogressionintrogressionColorpterin pigmentationSkin PigmentationDioxygenasesEvolutionsbiologiGeneticAnimalscarotenoid pigmentationPolymorphismPterin pigmentationEvolutionary BiologyPolymorphism GeneticBalanced polymorphism; Carotenoid pigmentation; Introgression; Podarcis muralis; Pterin pigmentation; Alcohol Oxidoreductases; Animals; Carotenoids; Color; Dioxygenases; Lizards; Pigmentation; Polymorphism Genetic; Pterins; Skin PigmentationPigmentationLizardsBiological SciencesCarotenoidsPterinsAlcohol OxidoreductasesPNAS PlusCarotenoid pigmentationPodarcis muralissense organs
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The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a lig…

1984

The structure and function of the 2-oxoglutarate binding site of prolyl 4-hydroxylase was studied by assaying the inhibitory potential of 24 selected aliphatic or aromatic compounds. All except one of them inhibited the enzyme competitively with respect to 2-oxoglutarate and noncompetitively with respect to Fe2+, the Ki values ranging from 0.8 microM to over 15 mM. The Ki values for the two most effective inhibitors, pyridine 2,5-dicarboxylate and 2,4-dicarboxylate, were about 0.8 microM and 2 microM, these compounds being the most potent inhibitors of prolyl 4-hydroxylase with respect to 2-oxoglutarate known so far. Only one of the compounds tested, 2-oxoadipinate, was able to support hydr…

chemistry.chemical_classificationCoordination sphereBinding SitesDecarboxylationStereochemistryIronProcollagen-Proline DioxygenaseChick EmbryoLigand (biochemistry)LigandsBiochemistryBinding CompetitiveDecarboxylationHydroxylationchemistry.chemical_compoundEnzymechemistryOxidoreductaseMoietyAnimalsKetoglutaric AcidsFerrous CompoundsBinding siteProtein BindingEuropean journal of biochemistry
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