Search results for "Escher"

showing 10 items of 728 documents

Escherichia coli inactivation by neutral solar heterogeneous photo-Fenton (HPF) over hybrid iron/montmorillonite/alginate beads

2015

Abstract Hybrid alginate montmorillonite iron enriched beads (Fe-MABs) were synthesized using ion gelation method and used as catalyst in Escherichia coli inactivation in neutral solar photo-Fenton conditions. A kinetic analysis showed that the E. coli inactivation by Fe-MABs followed a pseudo first-order kinetics model. Complete disinfection was achieved in 1 h of irradiation by using Fe-MABs in the presence of 10 ppm of H 2 O 2 . Preliminary studies on recyclability showed possible beads reused up to four times. Overall, Fe-MABs represent an environmental friendly material able to achieve bactericidal performance measured by E. coli inactivation under photooxidative conditions.

Iron alginate beadsWaste managementProcess Chemistry and TechnologyKineticsKinetic analysismedicine.disease_causeIron alginate beadEnvironmentally friendlyWater disinfectionPollutionHeterogeneous photo-FentonCatalysischemistry.chemical_compoundMontmorillonitechemistryEscherichia coli inactivationmedicineChemical Engineering (miscellaneous)IrradiationWater disinfectionEscherichia coliWaste Management and DisposalNuclear chemistryMontmorillonite
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Reduced Apo-Fumarate Nitrate Reductase Regulator (ApoFNR) as the Major Form of FNR in Aerobically Growing Escherichia coli▿

2008

ABSTRACT Under anoxic conditions, the Escherichia coli oxygen sensor FNR (fumarate nitrate reductase regulator) is in the active state and contains a [4Fe-4S] cluster. Oxygen converts [4Fe-4S]FNR to inactive [2Fe-2S]FNR. After prolonged exposure to air in vitro, apoFNR lacking a Fe-S cluster is formed. ApoFNR can be differentiated from Fe-S-containing forms by the accessibility of the five Cys thiol residues, four of which serve as ligands for the Fe-S cluster. The presence of apoFNR in aerobically and anaerobically grown E. coli was analyzed in situ using thiol reagents. In anaerobically and aerobically grown cells, the membrane-permeable monobromobimane labeled one to two and four Cys res…

Iron-Sulfur ProteinsAerobic bacteriamedicine.disease_causeNitrate reductaseMicrobiologymedicineEscherichia coliAnaerobiosisDisulfidesMolecular BiologyEscherichia colichemistry.chemical_classificationbiologySuccinate dehydrogenaseEscherichia coli Proteinsbiology.organism_classificationEnterobacteriaceaeEnzymes and ProteinsAerobiosisCulture MediaOxygenchemistryBiochemistryThiolbiology.proteinbacteriaAnaerobic bacteriaOxidation-ReductionBacteria
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Regulatory O 2 tensions for the synthesis of fermentation products in Escherichia coli and relation to aerobic respiration

1997

In an oxystat, the synthesis of the fermentation products formate, acetate, ethanol, lactate, and succinate of Escherichia coli was studied as a function of the O2 tension (pO2) in the medium. The pO2 values that gave rise to half-maximal synthesis of the products (pO0. 5) were 0.2-0.4 mbar for ethanol, acetate, and succinate, and 1 mbar for formate. The pO0.5 for the expression of the adhE gene encoding alcohol dehydrogenase was approximately 0.8 mbar. Thus, the pO2 for the onset of fermentation was distinctly lower than that for anaerobic respiration (pO0.5/= 5 mbar), which was determined earlier. An essential role for quinol oxidase bd in microaerobic growth was demonstrated. A mutant de…

Iron-Sulfur ProteinsAnaerobic respirationFormatesCellular respirationSuccinic AcidAcetatesBiologymedicine.disease_causeColiphagesBiochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundBioreactorsBacterial ProteinsMultienzyme ComplexesEscherichia coliGeneticsmedicineFormateAnaerobiosisMolecular BiologyEscherichia coliMixed acid fermentationAlcohol dehydrogenaseNitratesEthanolEthanolEscherichia coli ProteinsAlcohol DehydrogenaseGene Expression Regulation BacterialGeneral MedicineAldehyde OxidoreductasesAerobiosisArtificial Gene FusionOxygenRepressor ProteinsLac OperonchemistryBiochemistryFermentationLactatesbiology.proteinFermentationOxidoreductasesBacterial Outer Membrane ProteinsArchives of Microbiology
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O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli

1996

With an oxystat, changes in the pattern of expression of FNR-dependent genes from Escherichia coli were studied as a function of the O2 tension (pO2) in the medium. Expression of all four tested genes was decreased by increasing O2. However, the pO2 values that gave rise to half-maximal repression (pO(0.5)) were dependent on the particular promoter and varied between 1 and 5 millibars (1 bar = 10(5) Pa). The pO(0.5) value for the ArcA-regulated succinate dehydrogenase genes was in the same range (pO(0.5) = 4.6 millibars). At these pO2 values, the cytoplasm can be calculated to be well supplied with O2 by diffusion. Therefore, intracellular O2 could provide the signal to FNR, suggesting that…

Iron-Sulfur ProteinsCellular respirationRepressorBiologymedicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsGenes RegulatorEscherichia colimedicineAnaerobiosisMolecular BiologyEscherichia coliRegulation of gene expressionchemistry.chemical_classificationEscherichia coli ProteinsSuccinate dehydrogenaseMembrane ProteinsGene Expression Regulation BacterialElectron transport chainAerobiosisOxygenRepressor ProteinsSuccinate DehydrogenaseEnzymeLac OperonchemistryBiochemistryGenes BacterialMutationbiology.proteinOxidation-ReductionProtein KinasesIntracellularBacterial Outer Membrane ProteinsSignal TransductionResearch ArticleJournal of Bacteriology
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The Friedreich's Ataxia protein frataxin modulates DNA base excision repair in prokaryotes and mammals

2010

DNA-repair mechanisms enable cells to maintain their genetic information by protecting it from mutations that may cause malignant growth. Recent evidence suggests that specific DNA-repair enzymes contain ISCs (iron–sulfur clusters). The nuclearencoded protein frataxin is essential for the mitochondrial biosynthesis of ISCs. Frataxin deficiency causes a neurodegenerative disorder named Friedreich's ataxia in humans. Various types of cancer occurring at young age are associated with this disease, and hence with frataxin deficiency. Mice carrying a hepatocyte-specific disruption of the frataxin gene develop multiple liver tumours for unresolved reasons. In the present study, we show that frata…

Iron-Sulfur ProteinsDNA Repairmedicine.disease_causeBiochemistryDNA Glycosylases8-oxoG 78-dihydro-8-oxoguanineMice0302 clinical medicineIron-Binding Proteinsoxidative stressBER base excision repairCells CulturedMammalsMice Knockout0303 health sciencesfrataxinDMEM Dulbecco's modified Eagle's mediumbiologyLiver NeoplasmsSalmonella entericairon–sulfur clusterLife SciencesIron-binding proteinsTransfection3. Good healthLB Luria–BertaniOGG1 8-oxoguanine DNA glycosylase 1ISC iron–sulfur clusterFpg formamido-pyrimidine DNA glycosylaseHPRT hypoxanthine phosphoribosyltransferaseResearch ArticleDNA damageDNA repairSSB DNA single-strand breakTransfectionCell Line03 medical and health sciencesFRDA Friedreich's ataxiaROS reactive oxygen speciesmedicineAnimalsHumansMUTYH human mutY homologue (Escherichia coli)Molecular BiologyGene030304 developmental biologyFriedreich's ataxiaCell BiologyFibroblastsMolecular biologytumorigenesisProkaryotic CellsFriedreich AtaxiaDNA base excision repairDNA glycosylaseMutationHepatocytesFrataxinbiology.proteinInstitut für ErnährungswissenschaftCarcinogenesisMAPK mitogen-activated protein kinase030217 neurology & neurosurgeryDNA Damage
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O2-sensing and O2-dependent gene regulation in facultatively anaerobic bacteria.

1995

Availability of O2 is one of the most important regulatory signals in facultatively anaerobic bacteria. Various two- or one-component sensor/regulator systems control the expression of aerobic and anaerobic metabolism in response to O2. Most of the sensor proteins contain heme or Fe as cofactors that interact with O2 either by binding or by a redox reaction. The ArcA/ArcB regulator of aerobic metabolism in Escherichia coli may use a different sensory mechanism. In two-component regulators, the sensor is located in the cytoplasmic membrane, whereas one-component regulators are located in the cytoplasm. Under most conditions, O2 can readily reach the cytoplasm and could provide the signal in …

Iron-Sulfur ProteinsGram-Negative Facultatively Anaerobic RodsAnaerobic respirationRegulatorBiologymedicine.disease_causeBiochemistryMicrobiologychemistry.chemical_compoundBacterial ProteinsGeneticsmedicineMolecular BiologyHemeEscherichia coliRegulation of gene expressionSensory mechanismEscherichia coli ProteinsGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationOxygenchemistryBiochemistrybacteriaAnaerobic bacteriaBacteriaTranscription FactorsArchives of microbiology
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Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro.

2004

Abstract The oxygen sensor fumarate nitrate reductase regu-lator (FNR) of Escherichia coli contains in the active (anaerobic)state a [4Fe–4S] 2þ cluster which is lost after exposure to O 2 .Inaerobically prepared apoFNR, or in FNR obtained by treatmentof [4Fe–4S] FNR with O 2 in vitro, intramolecular cysteinedisulfides are found, including the cysteine residues which serveas ligands for the Fe–S cluster. It is shown here that thereconstitution of [4Fe–4S] FNR from this form of aerobicapoFNR was preceded by a long lag phase when glutathione wasused as the reducing agent. Addition of E. coli glutaredoxins(Grx) 1, 2 or 3 decreased the lag phase greatly and stimulatedthe reconstitution rate slig…

Iron-Sulfur ProteinsTime FactorsReducing agentFNRGlutaredoxinBiophysicsBiologyReductaseSulfidesmedicine.disease_causeNitrate reductaseBiochemistryOxygen sensorchemistry.chemical_compoundStructural BiologyGlutaredoxinGeneticsmedicineEscherichia coliCysteineDisulfidesThioredoxinMolecular BiologyEscherichia coliGlutaredoxinsDisulfide reductaseEscherichia coli ProteinsProteinsCell BiologyGlutathioneGlutathioneOxygenBiochemistrychemistryMultigene FamilyThioredoxinOxidoreductasesCysteineTranscription FactorsFEBS letters
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The oxygen-responsive transcriptional regulator FNR ofEscherichia coli : the search for signals and reactions

1997

The FNR (fumarate and nitrate reductase regulation) protein of Escherichia coli is an oxygen-responsive transcriptional regulator required for the switch from aerobic to anaerobic metabolism. In the absence of oxygen, FNR changes from the inactive to the active state. The sensory and the regulatory functions reside in separate domains of FNR. The sensory domain contains a Fe-S cluster, which is of the [4Fe-4S]2+ type under anaerobic conditions. It is suggested that oxygen is supplied to the cytoplasmic FNR by diffusion and inactivates FNR by direct interaction. Reactivation under anoxic conditions requires cellular reductants. In vitro, the Fe-S cluster is converted to a [3Fe-4S]+ or a [2Fe…

Iron-Sulfur Proteinsinorganic chemicalsEscherichia coli Proteinschemistry.chemical_elementBiologyNitrate reductasemedicine.disease_causeenvironment and public healthMicrobiologyOxygenMetabolic pathwayBacterial ProteinschemistryBiochemistryCytoplasmRespirationEscherichia coliTranscriptional regulationmedicinebacteriaSignal transductionMolecular BiologyEscherichia coliSignal TransductionTranscription FactorsMolecular Microbiology
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Hydrogen-producingEscherichia colistrains overexpressing lactose permease: FT-IR analysis of the lactose-induced stress

2014

The lactose permease gene (lacY) was overexpressed in the septuple knockout mutant of Escherichia coli, previously engineered for hydrogen production from glucose. It was expected that raising the lactose transporter activity would elevate the intracellular lactose concentration, inactivate the lactose repressor, induce the lactose operon, and as a result stimulate overall lactose consumption and conversion. However, overexpression of the lactose transporter caused a considerable growth delay in the recombinant strain on lactose, resembling to some extent the "lactose killing" phenomenon. Therefore, the recombinant strain was subjected to selection on lactose-containing media. Selection on …

Lactose permeasebiologyProcess Chemistry and TechnologyMutantBiomedical Engineeringlac operonBioengineeringGeneral MedicineLac repressormedicine.disease_causeApplied Microbiology and Biotechnologylaw.inventionchemistry.chemical_compoundBiochemistrychemistrylawDrug DiscoverymedicineRecombinant DNAAlpha-lactalbuminbiology.proteinMolecular MedicineLactoseEscherichia coliBiotechnologyBiotechnology and Applied Biochemistry
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Tetracycline inhibits the nitric oxide synthase activity induced by endotoxin in cultured murine macrophages

1998

Here we investigate the effects of tetracycline base and of a semi-synthetic tetracycline derivative, doxycycline, on the induction of inducible nitric oxide synthase and, hence, on the production of nitric oxide (NO) by lipopolysaccharide in J774 macrophage cultured in vitro. The treatment of J774 line with tetracycline base (6.25-250 microM) or doxycycline (5-50 microM) dose-dependently decreased the lipopolysaccharide-stimulated (1 microg/ml) inducible NO synthase activity and, consequently, nitrite formation. For instance, the inhibition was 70% for tetracycline base at 250 microM and 68% for doxycycline at 50 microM. The inhibitory effect of tetracyclines was due neither to a reduction…

LipopolysaccharideCell SurvivalTetracyclineBlotting WesternNitric Oxide Synthase Type IINitric oxideMicechemistry.chemical_compoundWestern blotPolysaccharidesEscherichia colimedicineAnimalsRNA MessengerAntibacterial agentPharmacologyDoxycyclinebiologymedicine.diagnostic_testMacrophagesBiological activityTetracyclineAnti-Bacterial AgentsEndotoxinsNitric oxide synthaseBiochemistrychemistryDoxycyclineEnzyme InductionProtein Biosynthesisbiology.proteinElectrophoresis Polyacrylamide GelNitric Oxide Synthasemedicine.drugEuropean Journal of Pharmacology
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