Search results for "REDUCTASE"

showing 10 items of 798 documents

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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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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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 oxidation of ubiquinol by the isolated rieske iron-sulfur protein in solution

1990

The pre-steady-state redox reactions of the Rieske iron-sulfur protein isolated from beef heart mitochondria have been characterized. The rates of oxidation by c-type cytochromes is much faster than the rate of reduction by ubiquinols. This enables the monitoring of the oxidation of ubiquinols by the Rieske protein through the steady-state electron transfer to cytochrome c in solution. The pH and ionic strength dependence of this reaction indicate that the ubiquinol anion is the direct reductant of the oxidized cluster of the iron-sulfur protein. The second electron from ubiquinol is diverted to oxygen by the isolated Rieske protein, and forms oxygen radicals that contribute to the steady-s…

Iron-Sulfur ProteinsUbiquinolCytochromeUbiquinoneBiophysicsmacromolecular substancesPhotochemistryBiochemistryRedoxMitochondria HeartElectron Transport Complex IIIElectron transferchemistry.chemical_compoundCytochrome C1AnimalsMolecular BiologybiologyChemistryCytochrome cHydrogen-Ion ConcentrationSolutionsKineticsCoenzyme Q – cytochrome c reductaseRieske proteinbiology.proteinCytochromesCattleOxidation-ReductionArchives of Biochemistry and Biophysics
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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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Step-by-step diagnosis and management of the nocebo/drucebo effect in statin-associated muscle symptoms patients: a position paper from the Internati…

2022

Statin intolerance is a clinical syndrome whereby adverse effects (AEs) associated with statin therapy [most commonly statin-associated muscle symptoms (SAMS)] result in the discontinuation of therapy and consequently increase the risk of adverse cardiovascular outcomes. However, complete statin intolerance occurs in only a small minority of treated patients (estimated prevalence of only 3-5%). Many perceived AEs are misattributed (e.g. physical musculoskeletal injury and inflammatory myopathies), and subjective symptoms occur as a result of the fact that patients expect them to do so when taking medicines (the nocebo/drucebo effect)-what might be truth even for over 50% of all patients wit…

KardiologiDrucebo effect Nocebo effect SAMS Statin intoleranceMusclesSAMSNocebo effectLipidsQPRSStatin intolerance.Muscular DiseasesStatin intolerancePhysiology (medical)Drucebo effectHumansOrthopedics and Sports MedicineCardiac and Cardiovascular SystemsHydroxymethylglutaryl-CoA Reductase Inhibitorsdrucebo effect ; nocebo effect ; SAMS ; statin intoleranceJournal of Cachexia Sarcopenia and Muscle
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Tigliane diterpenes from the latex of Euphorbia obtusifolia with inhibitory activity on the mammalian mitochondrial respiratory chain

2003

Abstract Six diterpenes isolated from the latex of Euphorbia obtusifolia Poir. (Euphorbiaceae) were evaluated for their inhibition of the NADH oxidase activity in submitochondrial particles from beef heart. 4,20-Dideoxyphorbol-12,13-bis(isobutyrate) was the most potent inhibitor and showed an inhibitory concentration with IC 50 value of 2.6±0.3 mM. In the present study, some structure–activity trends are suggested for the inhibitory activity of the mammalian mitochondrial respiratory chain of these natural product derivatives of 4-deoxyphorbol esters.

LatexStereochemistryRespiratory chainIn Vitro TechniquesMitochondria HeartElectron Transportchemistry.chemical_compoundEuphorbiaRotenoneDrug DiscoveryAnimalsNADH NADPH OxidoreductasesSubmitochondrial particlePharmacologyEuphorbiaOxidase testbiologyPlant ExtractsUncoupling AgentsEuphorbiaceaeBiological activitybiology.organism_classificationMitochondrial respiratory chainchemistryBiochemistryCattleDiterpenesDiterpeneJournal of Ethnopharmacology
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Supplementary Ultraviolet-B Radiation Induces a Rapid Reversal of the Diadinoxanthin Cycle in the Strong Light-Exposed DiatomPhaeodactylum tricornutu…

2002

AbstractA treatment of the diatom Phaeodactylum tricornutum with high light (HL) in the visible range led to the conversion of diadinoxanthin (Dd) to diatoxanthin (Dt). In a following treatment with HL plus supplementary ultraviolet (UV)-B, the Dt was rapidly epoxidized to Dd. Photosynthesis of the cells was inhibited under HL + UV-B. This is accounted for by direct damage by UV-B and damage because of the UV-B-induced reversal of the Dd cycle and the associated loss of photoprotection. The reversal of the Dd cycle by UV-B was faster in the presence of dithiothreitol, an inhibitor of the Dd de-epoxidase. Our results imply that the reversal of the Dd cycle by HL + UV-B was caused by an incre…

LightUltraviolet RaysPhysiologyPlant ScienceXanthophyllsBiologyPhotosynthesisThylakoidsDithiothreitolchemistry.chemical_compoundGeneticsPhaeodactylum tricornutumDiatomsDiadinoxanthinDiatoxanthinDarknessHydrogen-Ion ConcentrationAscorbic acidbiology.organism_classificationAdaptation PhysiologicalDithiothreitolBiochemistrychemistryThylakoidPhotoprotectionBiophysicsOxidoreductasesSignal TransductionResearch ArticlePlant Physiology
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Effects of carbamates as oxidative stressors on glutathione levels and lipid peroxidation in CHO-K1 cells

2006

Lipid peroxidationchemistry.chemical_compoundBiochemistryChemistryGlutathione reductaseGeneral MedicineGlutathioneOxidative phosphorylationToxicologyGPX4Toxicology Letters
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