Search results for "hydrogenase"

showing 10 items of 575 documents

Pyruvate dehydrogenase specific T cells in primary biliary cirrhosis show restricted antigen recognition sites

2002

:  Background/Aims: The aim was to characterise the antigen recognition sites of the variable T cell receptor α-chain (TCRAV) and β-chain (TCRBV) of T cells specific to the pyruvate dehydrogenase (PDC) in primary biliary cirrhosis. Methods: In 21 PDC-specific T cell clones isolated from five patients we analysed TCRAV and TCRBV usage by RT-PCR and sequenced the CDR3 regions. Results: Preferential expression of the TCR elements BV6 (6 clones), BV12 (4 clones) and BV1 (3 clones), and frequent usage of the joining elements JB2.3 and JB2.1 were seen. Analysis of the α chain revealed rearrangement of AV2 in 7 clones (35%) and AV7 in 3 clones, however, distribution of the joining elements was het…

HepatologyCell divisionT cellT-cell receptorhemic and immune systemsBiologymedicine.diseasePyruvate dehydrogenase complexMolecular biologyEpitopePrimary biliary cirrhosismedicine.anatomical_structureAntigenBiochemistrymedicineSequence motifLiver
researchProduct

How hexoses and inhibitors influence the malate transport system in Zygosaccharomyces bailii

1988

When grown in fructose or glucose the cells of Zygosaccharomyces bailii were physiologically different. Only the glucose grown cells (glucose cells) possessed an additional transport system for glucose and malate. Experiments with transport mutants had lead to the assumption that malate and glucose were transported by one carrier, but further experiments proved the existence of two separate carrier systems. Glucose was taken up by carriers with high and low affinity. Malate was only transported by an uptake system and it was not liberated by starved malate-loaded cells, probably due to the low affinity of the intracellular anion to the carrier. The uptake of malate was inhibited by fructose…

HexokinasebiologyZygosaccharomyces bailiiGlucose transporterFructoseGeneral MedicineMaltosebiology.organism_classificationBiochemistryMicrobiologyMalate dehydrogenasechemistry.chemical_compoundchemistryBiochemistryGeneticsMalate transportMolecular BiologyHexose transportArchives of Microbiology
researchProduct

Prehibernation and hibernation effects on the D-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orient…

2007

The D-3-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from liver jerboa (Jaculus orientalis), a ketone body converting enzyme in mitochondria, in two populations of mitochondria (heavy and light) has been studied in different jerboa states (euthermic, prehibernating and hibernating). The results reveal: (1) important variations between states in terms of ketones bodies, glucose and lipid levels; (2) significant differences between the BDH of the two mitochondrial populations in term of protein expression and kinetic properties. These results suggest that BDH leads an important conformational change depending on the physiological state of jerboa. This BDH structural change could be the c…

HibernationMESH: RatsMESH : HibernationMESH : Hydroxybutyrate DehydrogenaseMESH : RodentiaMESH: RodentiaFluorescent Antibody TechniqueMitochondria LiverRodentiaDehydrogenaseMitochondrionBiochemistryMESH : PhospholipidsHydroxybutyrate DehydrogenaseHibernation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsMESH: Animals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyInner mitochondrial membraneMESH: Fluorescent Antibody TechniqueJaculus orientalis[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyPhospholipidsMESH: Phospholipidschemistry.chemical_classificationMESH: KineticsbiologyMESH : RatsGeneral MedicineMetabolismbiology.organism_classificationRatsMESH: Hydroxybutyrate DehydrogenaseKineticsMESH : Fluorescent Antibody TechniqueEnzymechemistryBiochemistryMESH : Mitochondria LiverKetone bodiesMESH: Hibernationsense organsMESH : AnimalsMESH : KineticsMESH: Mitochondria Liver
researchProduct

Peroxisomal changes during hiberation of jerboa (Jaculus orientalis)

1998

As a member of the order of Rodentia, jerboa (Jaculus orientalis) is a natural deep hibernator and lives in subdesert highland in many parts of the world, including Morocco. Its small size (adult body weight ∼100 g), availability in the wild, tolerance to laboratory conditions, and some unique peroxisomal properties make it a suitable research subject for exploring peroxisome biogenesis under prehibernating and hibernating states. During 3 w, animals referred to as the prehibernator group were exposed to cold temperature (5 to 7°C) with food ad libitum. Part of the prehibernator group entered deep hibernation 24 to 48 h after starvation. Animals were sacrificed 4 and 6 d after starting hibe…

HibernationOxidase testmedicine.medical_specialtybiologyGeneral Chemical EngineeringOrganic ChemistryAcyl CoA dehydrogenaseUrate oxidaseMetabolismPeroxisomebiology.organism_classificationEndocrinologyInternal medicinebiology.proteinmedicineAcyl-CoA oxidaseJaculus orientalisJournal of the American Oil Chemists' Society
researchProduct

Peroxisome proliferator-activated receptors as regulators of lipid metabolism; tissue differential expression in adipose tissues during cold acclimat…

2004

Brown (BAT) and white (WAT) adipose tissues play a key role in the body energy balance orchestrated by the central nervous system. Hibernators have developed a seasonal obesity to respond to inhospitable environment. Jerboa is one of the deep hibernator originated from sub-desert highlands. Thus, this animal represents an excellent model to study cold adaptation mechanism. We report that the adipogenic factor PPARgamma exhibits a differential expression between BAT and WAT at mRNA level. A specific induction was only seen in WAT of pre-hibernating jerboa. Interestingly, PPAR beta/delta is specifically induced in BAT and brain of pre-hibernating jerboa, highlighting for the first time the po…

Hibernationmedicine.medical_specialtyAcclimatizationPeroxisome Proliferator-Activated ReceptorsPeroxisome proliferator-activated receptorAdipose tissueRodentiaWhite adipose tissueBiologyBiochemistryAcyl-CoA DehydrogenaseIon ChannelsMitochondrial ProteinsClofibric AcidInternal medicineHibernationBrown adipose tissuemedicineAcyl-CoA oxidaseAnimalsRNA MessengerUncoupling Protein 1chemistry.chemical_classificationFibric AcidsMembrane ProteinsGeneral MedicineLipid MetabolismLipidsMitochondriaCold TemperatureEndocrinologymedicine.anatomical_structurechemistryAdipose TissueGene Expression RegulationPhospholipasesCiprofibrateAcyl-CoA OxidaseCarrier ProteinsEnergy MetabolismOxidoreductasesThermogenesismedicine.drugBiochimie
researchProduct

Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system.

1998

ABSTRACT In Escherichia coli the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C 4 -dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase (DcuS) and a response regulator (DcuR). DcuS and DcuR are encoded by the dcuSR genes (previously yjdHG ) at 93.7 min on the calculated E. coli map. Inactivation of the dcuR and dcuS genes caused the loss of C 4 -dicarboxylate-stimulated synthesis of fumarate reductase ( frdABCD genes) and of the anaerobic fumarate-succinate antiporter DcuB ( dcuB gene). DcuS is predicted to contain a large periplasmic domain as the supposed site for C 4…

Histidine KinaseGenetics and Molecular Biologymedicine.disease_causeMicrobiologyAntiportersBacterial ProteinsFumaratesmedicineEscherichia coliDicarboxylic AcidsMolecular BiologyEscherichia coliRegulation of gene expressionDicarboxylic Acid TransportersbiologySuccinate dehydrogenaseEscherichia coli ProteinsHistidine kinaseMembrane ProteinsPeriplasmic spaceGene Expression Regulation BacterialFumarate reductaseTwo-component regulatory systemDNA-Binding ProteinsSuccinate DehydrogenaseResponse regulatorMutagenesis InsertionalBiochemistryGenes Bacterialbiology.proteinCarrier ProteinsProtein KinasesSignal TransductionTranscription FactorsJournal of bacteriology
researchProduct

Triazole-Containing [FeFe] Hydrogenase Mimics: Synthesis and Electrocatalytic Behavior

2019

Through a Cu-catalyzed Huisgen cycloaddition between terminal alkynes and azides (CuAAC) reaction, azide [(μ-SCH2)2N(4-N3C6H4)Fe2(CO)6] has demonstrated to be a robust and versatile reagent able to...

Hydrogenase010405 organic chemistryTriazole010402 general chemistry01 natural sciencesCombinatorial chemistryCycloaddition0104 chemical sciencesInorganic Chemistrychemistry.chemical_compoundchemistryReagentAzidePhysical and Theoretical ChemistryInorganic Chemistry
researchProduct

Application of 61Ni Mössbauer spectroscopy to chemical problems

1996

Using the possibility to produce 61Co sources at the MAinz MIcrotron, 61Ni Mossbauer spectroscopy was applied to different kinds of chemical problems. Measurements of isomer shifts and V zz values in some common compounds and compounds with unusual chemical bonding for comparison with band structure calculations, measurement of 61Ni Mossbauer parameters in model compounds for hydrogenase and dehydrogenase with an active [NiS4] centre, and study of novel binary NiF3 compounds at helium temperature are presented.

HydrogenaseMaterials scienceNuclear magnetic resonanceChemical bondMössbauer spectroscopyGeneral Physics and AstronomyPhysical chemistryMossbauer spectraElectronic band structureMicrotronHelium temperatureIl Nuovo Cimento D
researchProduct

Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism.

2002

Wolinella succinogenes performs oxidative phosphorylation with fumarate instead of O2 as terminal electron acceptor and H2 or formate as electron donors. Fumarate reduction by these donors ('fumarate respiration') is catalyzed by an electron transport chain in the bacterial membrane, and is coupled to the generation of an electrochemical proton potential (Deltap) across the bacterial membrane. The experimental evidence concerning the electron transport and its coupling to Deltap generation is reviewed in this article. The electron transport chain consists of fumarate reductase, menaquinone (MK) and either hydrogenase or formate dehydrogenase. Measurements indicate that the Deltap is generat…

HydrogenaseStereochemistryBiophysicsOxidative phosphorylationCoupling mechanismFormate dehydrogenaseBiochemistryCatalysisOxidative PhosphorylationWolinella succinogenesElectron Transportchemistry.chemical_compoundFumaratesHydrogenaseFormatechemistry.chemical_classificationFumarate respirationBinding SitesbiologySuccinate dehydrogenaseCell MembraneVitamin K 2Cell BiologyElectron acceptorFumarate reductaseElectron transport chainFormate DehydrogenasesWolinellaSuccinate DehydrogenaseBiochemistrychemistryModels Chemicalbiology.proteinFormate dehydrogenaseEnergy MetabolismOxidation-ReductionBacillus subtilisBiochimica et biophysica acta
researchProduct

Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina

2006

The mould Hypocrea jecorina (Trichoderma reesei) has two genes coding for enzymes with high similarity to the NADP-dependent glycerol dehydrogenase. These genes, called gld1 and gld2, were cloned and expressed in a heterologous host. The encoded proteins were purified and their kinetic properties characterized. GLD1 catalyses the conversion of d-glyceraldehyde and l-glyceraldehyde to glycerol, whereas GLD2 catalyses the conversion of dihydroxyacetone to glycerol. Both enzymes are specific for NADPH as a cofactor. The properties of GLD2 are similar to those of the previously described NADP-dependent glycerol-2- dehydrogenases (EC 1.1.1.156) purified from different mould species. It is a reve…

HypocreaDihydroxyacetoneGlyceraldehydeBiochemistrychemistry.chemical_compoundHypocreaGlyceraldehydeGlycerolCloning MolecularMolecular BiologyTrichoderma reeseichemistry.chemical_classificationbiologyGlycerol dehydrogenaseGlyceraldehyde-3-Phosphate DehydrogenasesHypocrea jecorinaCell Biologybiology.organism_classificationRecombinant ProteinsL-glyceraldehydeEnzymeGlycerol-3-phosphate dehydrogenasechemistryBiochemistryDihydroxyacetoneGlycerol dehydrogenaseNADP-specific glycerol dehydrogenaseNADPSugar Alcohol DehydrogenasesFEBS Journal
researchProduct