Search results for " Cytochrome c"

showing 10 items of 22 documents

The late Pleistocene origin of the Italian and Maltese populations of Potamon fluviatile (Malacostraca: Decapoda): insights from an expanded sampling…

2017

Evidence available for most inland water and terrestrial organisms highlights the significant role played by southern Italy, Sicily and the Maltese islands as refuges during Pleistocene climatic fluctuations. However, to date, the hypothesis that these areas may have acted as Pleistocene refugia for the freshwater crab Potamon fluviatile has not been explicitly tested, and a recent origin of local P. fluviatile populations was proposed on the basis of a small set of analysed molecular data. We have thus expanded the currently available data set on the population genetic structure of P. fluviatile through dedicated samplings in Sicily (Italy, 18 specimens), the Maltese Islands (Malta, 15 spe…

0106 biological sciences0301 basic medicineEarly PleistocenePleistoceneFreshwater crabs -- Maltarefuge areaPopulationSettore BIO/05 - Zoologiarefuge areasFreshwater crabs -- Italy010603 evolutionary biology01 natural sciences03 medical and health sciencesCytochrome oxidase -- CongressesMalacostracalcsh:Zoologylcsh:QL1-991educationFreshwater crabrange expansioneducation.field_of_studyPotamon fluviatilegeography.geographical_feature_categorybiologyEcologybiology.organism_classificationMitochondrial DNAlanguage.human_languageMaltese030104 developmental biologyGeographyArchipelagolanguageCytochromesAnimal Science and ZoologymtDNA Cytochrome c oxidase subunit I (COI)Freshwater crabThe European Zoological Journal
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mRNA-binding protein tristetraprolin is essential for cardiac response to iron deficiency by regulating mitochondrial function

2018

Cells respond to iron deficiency by activating iron-regulatory proteins to increase cellular iron uptake and availability. However, it is not clear how cells adapt to conditions when cellular iron uptake does not fully match iron demand. Here, we show that the mRNA-binding protein tristetraprolin (TTP) is induced by iron deficiency and degrades mRNAs of mitochondrial Fe/S-cluster-containing proteins, specifically Ndufs1 in complex I and Uqcrfs1 in complex III, to match the decrease in Fe/S-cluster availability. In the absence of TTP, Uqcrfs1 levels are not decreased in iron deficiency, resulting in nonfunctional complex III, electron leakage, and oxidative damage. Mice with deletion of Ttp …

0301 basic medicineCardiac responseCardiac function curveIron-Sulfur ProteinsTristetraprolinMitochondria HeartCell Line03 medical and health sciencesElectron Transport Complex IIIMiceTristetraprolinmedicineAnimalschemistry.chemical_classificationMice KnockoutReactive oxygen speciesMultidisciplinaryNDUFS1MyocardiumNADH DehydrogenaseIron deficiencyIron Deficienciesmedicine.diseaseCell biology030104 developmental biologychemistryPNAS PlusCoenzyme Q – cytochrome c reductaseOxidation-ReductionFunction (biology)
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Tor-Sch9 deficiency activates catabolism of the ketone body-like acetic acid to promote trehalose accumulation and longevity

2014

In mammals, extended periods of fasting leads to the accumulation of blood ketone bodies including acetoacetate. Here we show that similar to the conversion of leucine to acetoacetate in fasting mammals, starvation conditions induced ketone body-like acetic acid generation from leucine in S. cerevisiae. Whereas wild-type and ras2Δ cells accumulated acetic acid, long-lived tor1Δ and sch9Δ mutants rapidly depleted it through a mitochondrial acetate CoA transferase-dependent mechanism, which was essential for lifespan extension. The sch9Δ-dependent utilization of acetic acid also required coenzyme Q biosynthetic genes and promoted the accumulation of intracellular trehalose. These results indi…

AgingSaccharomyces cerevisiae ProteinsKetoneLongevitySaccharomyces cerevisiaeSaccharomyces cerevisiaePhosphatidylinositol 3-Kinaseschemistry.chemical_compoundAcetic acidSettore BIO/13 - Biologia ApplicataHumans2. Zero hungerchemistry.chemical_classificationbiologyCatabolismaging yeast nutrition acetic acid nutrientsTrehaloseOriginal ArticlesCell Biologybiology.organism_classificationchronological lifespanTrehaloseacetic acidSch9chemistryBiochemistryCoenzyme Q – cytochrome c reductaseKetone bodiesleucineLeucineProtein KinasesAging Cell
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Proton coupled electron transfer of ubiquinone Q2 incorporated in a self-assembled monolayer.

2011

We present a complete study of the reduction of ubiquinone Q(2) (UQ(2)) in simpler aqueous medium, over a pH range of 2.5 to 12.5. The short isoprenic chain ubiquinones (UQ(2)) were incorporated in a self-assembled monolayer. Under these conditions, the global 2e(-) electrochemical reaction can be described on the basis of a nine-member square scheme. The thermodynamic constants of the system were determined. The global 2e(-) process is controlled by the uptake of the second electron. The elementary electrochemical rate constants obtained by fitting of the experimental rate constant were k(s4) = 1.5 s(-1) for QH˙(+)(2)↔ QH(2), k(s5) = 1.5 s(-1) for QH˙↔ QH(-) and k(s6) = 1 s(-1) for Q˙(-)↔ …

Aqueous mediumChemistrySurface PropertiesUbiquinoneAnalytical chemistryGeneral Physics and AstronomyWaterSelf-assembled monolayerElectronHydrogen-Ion ConcentrationElectrochemistryElectron TransportReaction rate constantCoenzyme Q – cytochrome c reductaseMonolayerElectrochemistryThermodynamicsGoldPhysical and Theoretical ChemistryProton-coupled electron transferProtonsOxidation-ReductionPhysical chemistry chemical physics : PCCP
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Cytochrome c is released in a single step during apoptosis

2005

Release of cytochrome c from mitochondria is a central event in apoptotic signaling. In this study, we utilized a cytochrome c fusion that binds fluorescent biarsenical ligands (cytochrome c-4CYS (cyt. c-4CYS)) as well as cytochrome c-green fluorescent protein (cyt. c-GFP) to measure its release from mitochondria in different cell types during apoptosis. In single cells, the kinetics of cyt. c-4CYS release was indistinguishable from that of cyt. c-GFP in apoptotic cells expressing both molecules. Lowering the temperature by 7 degrees C did not affect this corelease, but further separated cytochrome c release from the subsequent decrease in mitochondrial membrane potential (DeltaPsi(m)). Cyt…

CytochromeUltraviolet RaysGreen Fluorescent ProteinsApoptosisLigandsMembrane PotentialsJurkat CellsCytochrome C1HumansCytochrome c oxidaseEnzyme InhibitorsMolecular BiologyProtein Synthesis InhibitorsMicroscopy VideobiologyTumor Necrosis Factor-alphaCytochrome bCytochrome cTemperatureCytochromes cCytochrome P450 reductaseCell BiologyStaurosporineMitochondriaCell biologyKineticsenzymes and coenzymes (carbohydrates)Coenzyme Q – cytochrome c reductaseDactinomycinbiology.proteinApoptosomeBiomarkersHeLa CellsCell Death & Differentiation
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A spontaneous mitonuclear epistasis converging on Rieske Fe-S protein exacerbates complex III deficiency in mice

2020

We previously observed an unexpected fivefold (35 vs. 200 days) difference in the survival of respiratory chain complex III (CIII) deficient Bcs1lp.S78G mice between two congenic backgrounds. Here, we identify a spontaneous homoplasmic mtDNA variant (m.G14904A, mt-Cybp.D254N), affecting the CIII subunit cytochrome b (MT-CYB), in the background with short survival. We utilize maternal inheritance of mtDNA to confirm this as the causative variant and show that it further decreases the low CIII activity in Bcs1lp.S78G tissues to below survival threshold by 35 days of age. Molecular dynamics simulations predict D254N to restrict the flexibility of MT-CYB ef loop, potentially affecting RISP dyna…

DYNAMICSepistasisMale0301 basic medicineNon-Mendelian inheritanceMitochondrial DiseasesMetabolic disordersRespiratory chainGeneral Physics and AstronomyDISEASEmitokondriotauditElectron Transport Complex IIIMice0302 clinical medicineenergy metabolismCRYSTAL-STRUCTUREIRON-SULFUR PROTEINlcsh:ScienceMice KnockoutGeneticsmitokondrio-DNAMultidisciplinaryCYTOCHROME BC(1) COMPLEXCytochrome bQCytochromes bMitochondria3. Good healthFemaleRESPIRATORY-CHAINGRACILE SYNDROMEhenkiinjääminenOxidation-ReductionMitochondrial DNAMitochondrial diseaseScienceCongenicMolecular Dynamics SimulationBiologyDNA MitochondrialArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesaineenvaihduntahäiriötmedicinemetabolic disordersAnimalsMUTATIONSEpistasis GeneticEnergy metabolismGeneral ChemistryCytochrome b Groupmedicine.diseaseMice Inbred C57BL030104 developmental biologyCoenzyme Q – cytochrome c reductaseEpistasis1182 Biochemistry cell and molecular biologyATPases Associated with Diverse Cellular ActivitiesEpistasislcsh:QGUI MEMBRANE-BUILDERkoe-eläinmallitMetabolism Inborn Errors030217 neurology & neurosurgeryGENERATIONMolecular ChaperonesNature Communications
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Effects of the herbicides Benzoylpropethyl and flampropisopropyl on rat liver mitochondria : an alteration in membrane fluidity ?

1984

Abstract The action of the herbicides benzoylpropethyl and flampropisopropyl, and the corresponding unesterified acids was studied in rat liver mitochondria. The herbicides were found to (a) inhibit the mitochondrial electron transfer in complex III or at the level of ubiquinone (I50 of 4 nmol mg protein−1 for flampropisopropyl and 18 for benzoylpropethyl with succinate as a substrate); (b) have an additional (however less sensitive) site of inhibition near succinate dehydrogenase; and (c) interfere with energy transfer. Sensitivity was increased 2- (benzoylpropethyl) and 3.5-fold (flampropisopropyl) as the rats age increased from 12–13 weeks to 23–26 weeks. The free acids were far less eff…

Health Toxicology and Mutagenesis[SDV]Life Sciences [q-bio]Mitochondrion03 medical and health sciencesElectron transfermedicineMembrane fluidityComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesbiologySuccinate dehydrogenaseBiological membrane04 agricultural and veterinary sciencesGeneral Medicine[SDV] Life Sciences [q-bio]BiochemistryMechanism of actionCoenzyme Q – cytochrome c reductaseToxicity040103 agronomy & agriculturebiology.protein0401 agriculture forestry and fisheriesRATmedicine.symptomAgronomy and Crop Science
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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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Regio- and stereoselective regulation of monooxygenase activities by isoenzyme-selective phosphorylation of cytochrome P450.

1989

The phosphorylation of the two major phenobarbital-inducible cytochrome P450 isoenzymes IIB1 and IIB2 was increased in hepatocytes by the action of the membrane permeating cAMP derivatives N6-dibutyryl-cAMP and 8-thiomethyl-cAMP. Under these conditions the dealkylation of 7-pentoxyresorufin, a selective substrate of cytochrome P450IIB1 and P450IIB2 was markedly reduced. 16 beta-Hydroxylation of testosterone which is catalyzed specifically only by cytochrome P450IIB1 and IIB2 was strongly reduced; for 16 alpha-hydroxylation which is also catalyzed by cytochrome P450IIB1 and IIB2 but additionally by 3 further cytochrome P450 isoenzymes, this reduction was less pronounced; for the oxidation of…

MaleCytochromeStereochemistry25-Hydroxyvitamin D3 1-alpha-hydroxylaseBiophysicsHydroxylationBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemCyclic AMPCytochrome c oxidaseAnimalsTestosteronePhosphorylationMolecular BiologybiologyChemistryCytochrome c peroxidaseCytochrome cCYP1A2Cytochrome P450 reductaseRats Inbred StrainsCell BiologyRatsIsoenzymesBiochemistryLiverSteroid 16-alpha-HydroxylaseCoenzyme Q – cytochrome c reductasePhenobarbitalbiology.proteinProtein Processing Post-TranslationalBiochemical and biophysical research communications
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Studies on the Biosynthesis of Microsomal Membrane Proteins. Site of Synthesis and Mode of Insertion of Cytochrome b5, Cytochrome b5 Reductase, Cytoc…

1982

The site of synthesis and mechanism of insertion into membranes of several microsomal polypeptides was studied using translation system programmed in vitro with polysomes or with mRNA extracted from free and membrane-bound rat liver polysomes. Primary translation products of cytochrome b5, NADH: cytochrome b5 oxidoreductase, NADPH: cytochrome P-450 oxidoreductase and epoxide hydrolase were isolated by specific immunoprecipitation and compared with the mature proteins. The following observations were made: 1 While cytochrome b5 and NADH: cytochrome b5 oxidoreductase are synthesized in free polysomes, NADPH: cytochrome P-450 oxidoreductase and epoxide hydrolase are made in membrane-bound poly…

MaleImmunodiffusionTime FactorsCytochromeBiochemistryElectron TransportCytochrome b5AnimalsCytochrome P450 family 1 member A1Epoxide hydrolaseCytochrome ReductasesCytochrome b5 reductaseNADPH-Ferrihemoprotein ReductaseEpoxide HydrolasesbiologyCytochrome bMembrane ProteinsCytochrome P450 reductaseRats Inbred StrainsMolecular biologyRatsCytochromes b5BiochemistryEnzyme InductionPhenobarbitalProtein BiosynthesisCoenzyme Q – cytochrome c reductaseMicrosomes Liverbiology.proteinCytochromesRabbitsCytochrome-B(5) ReductaseEuropean Journal of Biochemistry
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