Search results for "hydrogenase"

showing 10 items of 575 documents

The Cell Wall-Associated Glyceraldehyde-3-Phosphate Dehydrogenase of Candida albicans Is Also a Fibronectin and Laminin Binding Protein

1998

ABSTRACT By immunoelectron microscopy with a polyclonal antibody against the cytosolic glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Candida albicans (anti-GAPDH PAb), the protein was clearly detected at the outer surface of the cell wall, particularly on blastoconidia, as well as in the cytoplasm. Intact blastoconidia were able to adhere to fibronectin and laminin immobilized on microtiter plates, and this adhesion was markedly reduced by both the anti-GAPDH PAb and soluble GAPDH from Saccharomyces cerevisiae . In addition, semiquantitative flow cytometry analysis with the anti-GAPDH PAb showed a decrease in antibody binding to cells in the presence of soluble fib…

Immunoelectron microscopyImmunologyBiologyMicrobiologystomatognathic systemCell WallLamininCandida albicansMicroscopy ImmunoelectronCandida albicansGlyceraldehyde 3-phosphate dehydrogenaseBinding proteinGlyceraldehyde-3-Phosphate DehydrogenasesFlow Cytometrybiology.organism_classificationMolecular biologyCorpus albicansFibronectinsFibronectinInfectious DiseasesBiochemistryCytoplasmbiology.proteinParasitologyLamininFungal and Parasitic InfectionsCarrier ProteinsInfection and Immunity
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The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall protei…

2001

The authors show that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Saccharomyces cerevisiae, previously thought to be restricted to the cell interior, is also present in the cell wall. GAPDH activity, proportional to cell number and time of incubation, was detected in intact wild-type yeast cells. Intact cells of yeast strains containing insertion mutations in each of the three structural TDH genes (tdh1, tdh2 and tdh3) and double mutants (tdh1 tdh2 and tdh1 tdh3) also displayed a cell-wall-associated GAPDH activity, in the range of parental wild-type cells, although with significant differences among strains. A cell wall location of GAPDH was further confirmed …

Immunoelectron microscopySaccharomyces cerevisiaeCellBlotting WesternGenes FungalSaccharomyces cerevisiaeBiologyMicrobiologyCell wallstomatognathic systemBacterial ProteinsCell WallmedicineFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronGlyceraldehyde 3-phosphate dehydrogenaseGlyceraldehyde-3-Phosphate Dehydrogenasesbiology.organism_classificationFlow CytometryMolecular biologyYeastCulture MediaCytosolmedicine.anatomical_structureBiochemistryCytoplasmMutationbiology.proteinMicrobiology (Reading, England)
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Age-related changes of NADPH-diaphorase-positive neurons in the rat inferior colliculus and auditory cortex

2007

Nitric oxide (NO) has been implied in age-related changes of the central nervous system (CNS) and the central auditory pathway. The present study was conducted to investigate whether the number of NO-producing cells and their morphometric characteristics in the inferior colliculus (IC) and the auditory cortex (AC) are changed with the increasing age of the subjects. IC and AC sections of adult and senile Wistar rats were studied using the histochemical detection of NADPH-diaphorase activity (NADPH-d), a marker for neurons containing nitric oxide synthase (NOS). Our results showed a decreased area of the somas of NADPH-d-positive neurons in the dorsal cortex (DC) of the IC and a diffuse loss…

Inferior colliculusAgingAuditory PathwaysHistologyAuditory areaCentral nervous systemBiologyNADPH diaphoraseNitric OxideAuditory cortexNitric oxidechemistry.chemical_compoundmedicineAnimalsRats WistarInstrumentationAuditory CortexNeuronsNADPH DehydrogenaseRatsNitric oxide synthaseMedical Laboratory Technologymedicine.anatomical_structurechemistryAgeingbiology.proteinAnatomyNeuroscienceMicroscopy Research and Technique
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Na+ dependent glutamate transporters (EAAT1, EAAT2, and EAAT3) in primary astrocyte cultures: effect of oxidative stress.

2001

Abstract The Na + -dependent l -glutamate transporters EAAT1(GLAST), EAAT2 (GLT-1) and EAAT3 (EAAC1) are expressed in primary astrocyte cultures, showing that the EAAT3 transporter is not neuron-specific. The presence of these three transporters was evaluated by RT–PCR, immunoblotting, immunocytochemical techniques, and transport activity. When primary astrocyte cultures were incubated with l -buthionine-( S , R )-sulfoximine (BSO), a selective inhibitor of γ-glutamylcysteine synthetase, the GSH concentration was significantly lower than in control cultures, but the expression and amount of protein of EAAT1, EAAT2 and EAAT3 and transport of l -glutamate was unchanged. Oxidative stress was c…

InsecticidesAmino Acid Transport System X-AGImmunoblottingGlutamic AcidOxidative phosphorylationBiologymedicine.disease_causeDDTchemistry.chemical_compoundGlutamate Plasma Membrane Transport ProteinsLactate dehydrogenasemedicineAnimalsRNA MessengerRats WistarMolecular BiologyCells CulturedBrain ChemistryL-Lactate DehydrogenaseSymportersReverse Transcriptase Polymerase Chain ReactionGeneral NeuroscienceSodiumGlutamate receptorTransporterGlutathioneGlutathioneImmunohistochemistryRatsExcitatory Amino Acid Transporter 1Oxidative Stressmedicine.anatomical_structureExcitatory Amino Acid Transporter 3BiochemistrychemistryAnimals NewbornExcitatory Amino Acid Transporter 2Microscopy FluorescenceAstrocytesNeurogliaElectrophoresis Polyacrylamide GelNeurology (clinical)Carrier ProteinsOxidative stressDevelopmental BiologyAstrocyteBrain research
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Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors a…

1995

The promoter region and transcriptional regulation of the nuoA-N gene locus encoding the proton-translocating NADH:quinone oxidoreductase was analysed. A 560 bp intergenic region upstream of the nuo locus was followed by a gene (designated lrhA for LysR homologue A) coding for a gene regulator similar to those of the LysR family. Disruption of lrhA did not affect growth (respiratory or non-respiratory) or expression of nuo significantly. Transcriptional regulation of nuo by electron acceptors, electron donors and the transcriptional regulators ArcA, FNR, NarL and NarP, and by IHF (integration host factor) was studied with protein and operon fusions containing the promoter region up to base …

Integration Host FactorsIron-Sulfur ProteinsTranscription GeneticOperonMolecular Sequence DataRepressorLocus (genetics)medicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsOperonmedicineTranscriptional regulationEscherichia coliAmino Acid SequencePromoter Regions GeneticMolecular BiologyEscherichia coliGenebiologyBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsNADH dehydrogenasePromoterNADH DehydrogenaseGene Expression Regulation BacterialMolecular biologyAerobiosisDNA-Binding ProteinsRepressor ProteinsBiochemistrybiology.proteinbacteriaProtonsSequence AlignmentBacterial Outer Membrane ProteinsTranscription FactorsMolecular microbiology
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Intramolecular electron transfer between molybdenum and iron mimicking bacterial sulphite dehydrogenase

2014

Diferrocenyl/diferrocenium substituted dioxido molybdenum(VI) complexes [Fe2MoO2] 2(Fc)/[2(FC)]²⁺ mimic the catalytic active site including the redox subunits as well as the catalytic function of bacterial sulphite oxidases.

IronSulfite DehydrogenaseMolecular Conformationchemistry.chemical_elementBiocompatible MaterialsElectronsCrystallography X-RayPhotochemistryRedoxCatalysisCatalysisElectron TransportElectron transferCoordination ComplexesCatalytic DomainPolymer chemistryMaterials ChemistrySulfite dehydrogenaseFerrous CompoundsMolybdenumBacteriabiologyMetals and AlloysActive siteGeneral ChemistryElectron transport chainSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryMolybdenumIntramolecular forceCeramics and Compositesbiology.proteinOxidation-ReductionChemical Communications
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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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Respiratory behaviour of a Zymomonas mobilis adhB::kan(r) mutant supports the hypothesis of two alcohol dehydrogenase isoenzymes catalysing opposite …

2006

AbstractPerturbation of the aerobic steady-state in a chemostat culture of the ethanol-producing bacterium Zymomonas mobilis with a small pulse of ethanol causes a burst of ethanol oxidation, although the reactant ratio of the alcohol dehydrogenase (ADH) reaction ([NADH][acetaldehyde][H+])/([ethanol][NAD+]) remains above the Keq value. Simultaneous catalysis of ethanol synthesis and oxidation by the two ADH isoenzymes, residing in different redox microenvironments, has been proposed previously. In the present study, this hypothesis is verified by construction of an ADH-deficient strain and by demonstration that it lacks the oxidative burst in response to perturbation of its aerobic steady-s…

Kanamycin ResistanceBiophysicsMetabolic channellingChemostatBiochemistryRedoxZymomonas mobilisModels BiologicalCatalysischemistry.chemical_compoundContinuous cultureStructural BiologyGeneticsEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolbiologyEthanolChemistryRespirationZymomonas mobilisAcetaldehydeAlcohol DehydrogenaseCell Biologybiology.organism_classificationAerobiosisIsoenzymesKineticsBiochemistrybiology.proteinMutant ProteinsNAD+ kinaseFEBS letters
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