Search results for " cytochrome c"

showing 10 items of 22 documents

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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Effects of vitamin A deficiency on mitochondrial function in rat liver and heart.

2000

The aim of this study was to investigate comparative effects of vitamin A deficiency on respiratory activity and structural integrity in liver and heart mitochondria. Male rats were fed a liquid control diet (control rats) or a liquid vitamin A-deficient diet (vitamin A-deficient rats) for 50 days. One group of vitamin-A deficient rats was refed a control diet for 15 days (vitamin A-recovered rats). To assess the respiratory function of mitochondria the contents of coenzyme Q (ubiquinone, CoQ), cytochrome c and the activities of the whole electron transport chain and of each of its respiratory complexes were evaluated. Chronic vitamin A deficiency promoted a significant increase in the endo…

VitaminMalemedicine.medical_specialtyUbiquinoneRespiratory chainMedicine (miscellaneous)Cytochrome c GroupMitochondria LiverMitochondria HeartElectron Transportchemistry.chemical_compoundRetinoidsInternal medicinemedicineAnimalsVitamin ERespiratory functionNutrition and DieteticsbiologyVitamin A DeficiencyCytochrome cRetinolmedicine.diseaseRatsVitamin A deficiencyEndocrinologyMitochondrial respiratory chainchemistryCoenzyme Q – cytochrome c reductasebiology.proteinThe British journal of nutrition
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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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Analogues of cytotoxic squamocin using reliable reactions: new insights into the reactivity and role of the α,β-unsaturated lactone of the annonaceou…

2006

Abstract A small library of squamocin analogues has been prepared and screened biologically (cytotoxicity, inhibition of mitochondrial complex I and complex III). To centre diversity on a crucial part of the molecule (i.e., the α,β-unsaturated lactone), an original and reliable lactone opening reaction has been discovered and exploited among other efficient reactions.

chemistry.chemical_classificationStereochemistryOrganic ChemistryBiochemistrychemistryCoenzyme Q – cytochrome c reductaseDrug DiscoveryClick chemistryMoleculeCytotoxic T cellReactivity (chemistry)Annonaceous AcetogeninsCytotoxicityLactoneTetrahedron
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Structure of the Zymomonas mobilis respiratory chain: oxygen affinity of electron transport and the role of cytochrome c peroxidase

2014

The genome of the ethanol-producing bacterium Zymomonas mobilis encodes a bd-type terminal oxidase, cytochrome bc 1 complex and several c-type cytochromes, yet lacks sequences homologous to any of the known bacterial cytochrome c oxidase genes. Recently, it was suggested that a putative respiratory cytochrome c peroxidase, receiving electrons from the cytochrome bc 1 complex via cytochrome c 552, might function as a peroxidase and/or an alternative oxidase. The present study was designed to test this hypothesis, by construction of a cytochrome c peroxidase mutant (Zm6-perC), and comparison of its properties with those of a mutant defective in the cytochrome b subunit of the bc 1 complex (Zm…

ZymomonasbiologyCytochrome bc1Cytochrome c peroxidaseCytochrome cCytochrome dCytochrome-c PeroxidaseMicrobiologyMolecular biologyStandardElectron TransportOxygenBiochemistryCytochrome C1Coenzyme Q – cytochrome c reductasebiology.proteinCytochrome c oxidaseOxidoreductasesPhysiology and BiochemistryGene DeletionPeroxidaseMicrobiology
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Membrane D-lactate oxidase in Zymomonas mobilis: evidence for a branched respiratory chain.

1998

Respiratory chain composition of the ethanol-producing bacterium Zymomonas mobilis was studied. Its membrane D-lactate oxidase was characterised. With NADH, but not D-lactate as substrate, a cytochrome o-like component was seen in CO difference spectra. Chlorpromazine specifically inhibited reduction of cytochrome d, while myxothiazol eliminated the cytochrome o-like features in CO difference spectra. It is suggested that electrons from NADH are distributed between branches terminated by the cytochrome o-like component, cytochrome a, and cytochrome d. With D-lactate, electrons are transported to cytochrome a, or an unidentified CN(-)-sensitive oxidase, and cytochrome d.

StereochemistryChlorpromazineMicrobiologyMixed Function OxygenasesElectron Transportchemistry.chemical_compoundOxygen ConsumptionCytochrome C1Multienzyme ComplexesGeneticsCytochrome c oxidaseNADH NADPH OxidoreductasesLactic AcidMolecular BiologyZymomonasbiologyMyxothiazolCytochrome b6f complexCytochrome bCytochrome cCytochrome dNADAerobiosisThiazolesBiochemistrychemistrySpectrophotometryCoenzyme Q – cytochrome c reductasebiology.proteinCytochromesMethacrylatesOxidation-ReductionFEMS microbiology letters
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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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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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One Enzyme, Two Functions

2010

The human enzyme paraoxonase-2 (PON2) has two functions, an enzymatic lactonase activity and the reduction of intracellular oxidative stress. As a lactonase, it dominantly hydrolyzes bacterial signaling molecule 3OC12 and may contribute to the defense against pathogenic Pseudomonas aeruginosa. By its anti-oxidative effect, PON2 reduces cellular oxidative damage and influences redox signaling, which promotes cell survival. This may be appreciated but also deleterious given that high PON2 levels reduce atherosclerosis but may stabilize tumor cells. Here we addressed the unknown mechanisms and linkage of PON2 enzymatic and anti-oxidative function. We demonstrate that PON2 indirectly but specif…

chemistry.chemical_classificationReactive oxygen speciesbiologySuperoxideCytochrome cParaoxonaseCell BiologyMitochondrionBiochemistrychemistry.chemical_compoundchemistryBiochemistryCoenzyme Q – cytochrome c reductasebiology.proteinLactonaseInner mitochondrial membraneMolecular BiologyJournal of Biological Chemistry
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