Search results for "Electron transport"

showing 10 items of 237 documents

Application of 3-Quinolinoyl Picket Porphyrins to the Electroreduction of Dioxygen to Water: Mimicking the Active Site of Cytochromec Oxidase

2001

International audience

PorphyrinsHemeproteinReducing agentIronchemistry.chemical_elementPhotochemistryElectrochemistry[ CHIM ] Chemical SciencesBiochemistryOxygenElectron Transport Complex IVO-O activationcytochrome c oxidase[CHIM]Chemical SciencesCytochrome c oxidaseBinding siteMolecular BiologyComputingMilieux_MISCELLANEOUSBinding SitesbiologyChemistryMolecular MimicryOrganic ChemistryActive siteElectron Transport Complex IVheme proteinsoxidoreductasesOxygenelectrochemistryReducing Agentsbiology.proteinMolecular MedicineIndicators and ReagentsSpectrophotometry UltravioletOxidation-ReductionCopperChemBioChem
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Phylogenetic relationship among genera of Polymorphidae (Acanthocephala), inferred from nuclear and mitochondrial gene sequences.

2013

Abstract Acanthocephalans of the family Polymorphidae Meyer, 1931 are obligate endoparasites with complex life cycles. These worms use vertebrates (marine mammals, fish-eating birds and waterfowl) as definitive hosts and invertebrates (amphipods, decapods and euphausiids) as intermediate hosts to complete their life cycle. Polymorphidae has a wordwide distribution, containing 12 genera, with approximately 127 species. The family is diagnosed by having a spinose trunk, bulbose proboscis, double-walled proboscis receptacle, and usually four to eight tubular cement glands. To conduct a phylogenetic analysis, in the current study sequences of the small (18S) and large-subunit (28S) ribosomal RN…

ProfilicollisZoologyBiologyAcanthocephalaPolymorphidaeElectron Transport Complex IVEvolution MolecularMonophylyPhylogeneticsRNA Ribosomal 28SGeneticsRNA Ribosomal 18SAnimalsMolecular BiologyEcology Evolution Behavior and SystematicsGenes HelminthPhylogenyLikelihood FunctionsPhylogenetic treeModels GeneticBayes Theorembiology.organism_classificationMaximum parsimonyGenes MitochondrialCladogramRNA HelminthAcanthocephalaMultilocus Sequence TypingMolecular phylogenetics and evolution
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Proteins participating to the post-transcriptional regulation of the mitochondrial cytochrome c oxidase subunit IV via elements located in the 3′UTR

2009

Abstract In developing rat brain cytochrome c oxidase subunit IV (COXIV) expression is also regulated at post-transcriptional level and two 3′UTR-COXIV RNA-binding factors have been identified. Here, we report the enrichment and identification of the factors from just born rat brains by affinity chromatography of biotinylated 3′UTR-COXIV RNA–protein complexes on streptavidin-conjugated paramagnetic particles. We successfully isolated two main proteins of about 86 and 42 kDa, whose sequences were highly attributable to Hsp90 and Actin. The purified proteins maintain RNA-binding ability and specificity for COXIV messenger and, interacting with the 3′UTR, then could negatively modulate mRNA tr…

Protein subunitRNA-binding proteinMitochondrionChromatography AffinityElectron Transport Complex IVMitochondrial ProteinsRats Sprague-DawleySequence Analysis ProteinSerineAnimalsCytochrome c oxidaseHSP90 Heat-Shock ProteinsPhosphorylationPost-transcriptional regulation RNA-binding proteins Mitochondria Cytochrome c oxidase COXIV 3'UTR3' Untranslated RegionsMolecular BiologyPost-transcriptional regulationMessenger RNAbiologyThree prime untranslated regionBrainRNA-Binding ProteinsTranslation (biology)Cell BiologyActinsRatsMolecular WeightAnimals NewbornGene Expression RegulationBiochemistrybiology.proteinMolecular MedicineProtein BindingMitochondrion
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Proteomics evaluation of enniatins acute toxicity in rat liver

2021

Abstract Enniatins (ENs) are emerging mycotoxins produced by Fusarium fungi which are cytotoxic also at low concentrations due to its ionophoric properties. The aim of this study was to evaluate the hepatic toxicity of ENs exposure at different concentrations in Wistar rats through a proteomic approach. Animals were intoxicated by oral gavage with medium (EN A 256, ENA1 353, ENB 540, ENB1 296 μg/mL) and high concentrations (ENA 513, ENA1 706, ENB 1021, ENB1 593 μg/mL) of an ENs mixture and sacrificed after 8 h. Protein extraction was performed using powdered liver. Peptides were analyzed using a liquid chromatography coupled with a quadrupole time-of-flight mass spectrometer. Proteins were …

ProteomicsFusariumToxicologyProteomicsmedicine.disease_cause03 medical and health sciences0404 agricultural biotechnologyTandem Mass SpectrometryIn vivoDepsipeptidesIn vivoProtein purificationmedicineAnimalsRats Wistar030304 developmental biology0303 health sciencesbiologyChemistry04 agricultural and veterinary sciencesGeneral MedicineMetabolismMycotoxinsbiology.organism_classification040401 food scienceAcute toxicityRatsLiverBiochemistryOxidative stressElectron transport chainFemaleNAD+ kinaseBiomarkersOxidative stressChromatography LiquidFood ScienceFood and Chemical Toxicology
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Mitochondrial proteomics profile points oxidative phosphorylation as main target for beauvericin and enniatin B mixture

2020

Abstract Beauvericin (BEA) and enniatin B (EN B) are non-legislated Fusarium mycotoxins usually found in cereal and cereal-based products all around the world. By the proteomic analysis of mitochondria enriched extracts from Jurkat cells exposed for 24 h to three concentrations of BEA:EN B (0.01–0.1–0.5 μM), a number of 1821 proteins (202 mitochondrial) were identified and relatively quantified. 340 proteins (59 mitochondrial) were statistically significant altered in our samples (Anova p-value ≤ 0.05 and fold change (FC) ≥1.5). The protein mitochondrial translational release factor 1 like (MTRF1L) was the most abundant protein in the three mycotoxin exposures studied. The mycotoxins mixtur…

ProteomicsTranscription GeneticOxidative phosphorylationMitochondrionToxicologyProteomicsRibosomeJurkat cellsOxidative PhosphorylationElectron TransportMitochondrial ProteinsJurkat Cells03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyDepsipeptidesHumans030304 developmental biology0303 health sciencesfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceBeauvericinFold changeMitochondriachemistryBiochemistryBacterial outer membraneFood ScienceFood and Chemical Toxicology
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Synthesis of pyrido[2,1-a]isoquinolin-4-ones and oxazino[2,3-a]isoquinolin-4-ones: New inhibitors of mitochondrial respiratory chain

2013

International audience; Benzo[a]quinolizine is an important heterocyclic framework that can be found in numerous bioactive compounds. The general scheme for the synthesis of these compounds was based on the preparation of the appropriate dihydroisoquinolines by Bischler-Napieralski cyclization with good yields, followed by the Pemberton method to form the oxazinones or pyridones derivatives via acyl-ketene imine cyclocondensation. All the synthesized compounds were assayed in vitro for their ability to inhibit mitochondrial respiratory chain. Most of the tested compounds were able to inhibit the integrated electron transfer chain, measured as NADH oxidation, which includes complexes I, III …

PyridonesStereochemistryImine010402 general chemistryRing (chemistry)01 natural sciencesMitochondria HeartElectron TransportStructure-Activity Relationshipchemistry.chemical_compoundMultienzyme ComplexesFuranOxazinesDrug DiscoveryAnimalsNADH NADPH OxidoreductasesCytotoxicityPharmacologyDose-Response Relationship DrugMolecular Structure[CHIM.ORGA]Chemical Sciences/Organic chemistry010405 organic chemistryOrganic ChemistryQuinolizineBiological activityGeneral MedicineIsoquinolinesElectron transport chain3. Good health0104 chemical sciencesMitochondrial respiratory chainchemistryCattleEuropean Journal of Medicinal Chemistry
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The mitochondrial genome of Schizosaccharomyces pombe. Stimulation of intra-chromosomal recombination in Escherichia coli by the gene product of the …

1991

The open reading frame of the first intron of the mitochondrial cox1 gene (cox1I1) was expressed in Escherichia coli. The putative intron-encoded protein stimulated the formation of intra-chromosomal lac +-recombinants about threefold. No stimulation was found when the reading frame was inserted in the opposite direction, or when it was interrupted by a deletion. The intronic open reading frame did not complement recA − or recB − mutants of E. coli. In S. pombe, elimination of this intron did not abolish homologous recombination in mitochondria. A possible role of the recombinase activity in yeast mitochondria will be discussed.

RNA SplicingGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeBiologymedicine.disease_causeDNA MitochondrialElectron Transport Complex IVFungal ProteinsRecombinasesOpen Reading FramesSequence Homology Nucleic AcidEndoribonucleasesSchizosaccharomycesGeneticsmedicineRecombinaseEscherichia coliAmino Acid SequenceDNA FungalEscherichia coliRecBCDRecombination GeneticRecombinase activityBase SequenceIntegrasesIntronGeneral Medicinebiology.organism_classificationMolecular biologyNucleotidyltransferasesIntronsOpen reading frameSchizosaccharomyces pombeDNA NucleotidyltransferasesbacteriaHomologous recombination
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Oxygen regulated gene expression in facultatively anaerobic bacteria

1994

In facultatively anaerobic bacteria such as Escherichia coli, oxygen and other electron acceptors fundamentally influence catabolic and anabolic pathways. E. coli is able to grow aerobically by respiration and in the absence of O2 by anaerobic respiration with nitrate, nitrite, fumarate, dimethylsulfoxide and trimethylamine N-oxide as acceptors or by fermentation. The expression of the various catabolic pathways occurs according to a hierarchy with 3 or 4 levels. Aerobic respiration at the highest level is followed by nitrate respiration (level 2), anaerobic respiration with the other acceptors (level 3) and fermentation. In other bacteria, different regulatory cascades with other underlyin…

Regulation of gene expressionAnaerobic respirationAnabolismCellular respirationGene Expression Regulation BacterialGeneral MedicineBiologymedicine.disease_causeMicrobiologyAerobiosisElectron TransportOxygenBacteria AnaerobicOxidative StressGlucoseBiochemistrymedicineFermentationAnaerobiosisAnaerobic bacteriaEnergy MetabolismMolecular BiologyEscherichia coliAnaerobic exerciseNitritesAntonie van Leeuwenhoek
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Adaptive antioxidant methionine accumulation in respiratory chain complexes explains the use of a deviant genetic code in mitochondria

2008

Humans and most other animals use 2 different genetic codes to translate their hereditary information: the standard code for nuclear-encoded proteins and a modern variant of this code in mitochondria. Despite the pivotal role of the genetic code for cell biology, the functional significance of the deviant mitochondrial code has remained enigmatic since its first description in 1979. Here, we show that profound and functionally beneficial alterations on the encoded protein level were causative for the AUA codon reassignment from isoleucine to methionine observed in most mitochondrial lineages. We demonstrate that this codon reassignment leads to a massive accumulation of the easily oxidized …

Respiratory chainOxidative phosphorylationMitochondrionBiologyDNA MitochondrialGenomeAntioxidantsElectron Transportchemistry.chemical_compoundMethionineAnimalsIsoleucineInner mitochondrial membraneGeneticschemistry.chemical_classificationGenomeMultidisciplinaryMethionineFungiPlantsBiological SciencesGenetic codeBiological EvolutionAmino acidOxidative StresschemistryGenetic CodeMitochondrial MembranesDatabases Nucleic AcidProceedings of the National Academy of Sciences
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Photoinduced Electron Transfer in Multiporphyrinic Interlocked Structures: The Effect of Copper(I) Coordination in the Central Site

2004

Photoinduced processes have been determined in a [2]catenane containing a zinc(II) porphyrin, a gold(III) porphyrin, and two free phenanthroline binding sites, Zn-Au(+), and in the corresponding copper(I) phenanthroline complex, Zn-Cu(+)-Au(+). In acetonitrile solution Zn-Au(+) is present in two different conformations: an extended one, L, which accounts for 40 % of the total, and a compact one, S. In the L conformation, the electron transfer from the excited state of the Zn porphyrin to the gold-porphyrin unit (k = 1.3x10(9) s(-1)) is followed by a slow recombination (k = 8.3x10(7) s(-1)) to the ground state. The processes in the S conformation cannot be clearly resolved but a charge-separ…

RotaxanesMetalloporphyrinsPhotochemistryPhenanthrolineCatenaneMolecular Conformationchemistry.chemical_elementElectronsPhotochemistryCatalysisPhotoinduced electron transferElectron Transportchemistry.chemical_compoundElectron transferChemistryOrganic ChemistryGeneral ChemistryPorphyrinCopperZincCrystallographyEnergy TransferSpectrophotometryExcited stateGoldGround stateCopperChemistry - A European Journal
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