Search results for "hydrogenase"

showing 10 items of 575 documents

Mitochondrial aldehyde dehydrogenase (ALDH-2)--maker of and marker for nitrate tolerance in response to nitroglycerin treatment.

2008

The hemodynamic and anti-ischemic effects of nitroglycerin (GTN) are rapidly blunted as a result of the development of nitrate tolerance. Long-term nitrate treatment also is associated with decreased vascular responsiveness caused by changes in intrinsic mechanisms of the tolerant vasculature itself. According to the oxidative stress concept, increased vascular superoxide and peroxynitrite production as well as an increased sensitivity to vasoconstrictors secondary to activation of protein kinase C as well as vascular NADPH oxidases contribute to the development of tolerance. Recent experimental work has defined new tolerance mechanisms, including inhibition of the enzyme that bioactivates …

Aldehyde dehydrogenasePharmacologyToxicologymedicine.disease_causeProstacyclin synthasechemistry.chemical_compoundNitroglycerinDrug tolerancemedicineHumansEndothelial dysfunctionchemistry.chemical_classificationReactive oxygen speciesNitratesbiologyAldehyde Dehydrogenase MitochondrialGeneral MedicineDrug ToleranceAldehyde Dehydrogenasemedicine.diseaseMitochondriaOxidative StresschemistryBiochemistrycardiovascular systembiology.proteinSoluble guanylyl cyclasePeroxynitriteOxidative stresscirculatory and respiratory physiologyChemico-biological interactions
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Alkylation at the active site of the D-3-hydroxybutyrate dehydrogenase (BDH), a membrane phospholipid-dependent enzyme, by 3-chloroacetyl pyridine ad…

1997

The structure of the rat liver's D-3-hydroxybutyrate dehydrogenase (BDH) active site has been investigated using an affinity alkylating reagent, the 3-chloroacetyl pyridine adenine dinucleotide (3-CAPAD). This NAD+ analogue reagent strongly inactivates the enzyme following a concentration- and time-dependent process with a stoichiometry of approximately 1. The reagent reacts at the coenzyme binding site as revealed by the efficient protection by NADH. The effect of 3-CAPAD is stronger with the enzyme into its natural membrane environment than with the lipid-free purified apoBDH or with the reconstituted apoBDH-mitochondrial phospholipid complex. The pH-dependent effect on the inactivation p…

AlkylationStereochemistryAffinity labelMitochondria LiverDehydrogenaseBiochemistryHydroxybutyrate DehydrogenaseMembrane LipidsAnimalsCoenzyme bindingCysteineBinding sitePhospholipidsBinding SitesAffinity labelingMolecular StructurebiologyChemistryActive siteAffinity LabelsGeneral MedicineNADRatsReagentLinear Modelsbiology.proteinNAD+ kinaseBiochimie
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Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications

1997

In Escherichia coli the expression of the nuo genes encoding the proton pumping NADH dehydrogenase I is stimulated by the presence of fumarate during anaerobic respiration. The regulatory sites required for the induction by fumarate, nitrate and O2 are located at positions around –309, –277, and downstream of –231 bp, respectively, relative to the transcriptional-start site. The fumarate regulator has to be different from the O2 and nitrate regulators ArcA and NarL. For growth by fumarate respiration, the presence of NADH dehydrogenase I was essential, in contrast to aerobic or nitrate respiration which used preferentially NADH dehydrogenase II. The electron transport from NADH to fumarate …

Anaerobic respirationAcetatesmedicine.disease_causeBiochemistryElectron TransportFumaratesEscherichia colimedicineDimethyl SulfoxideNADH NADPH OxidoreductasesAnaerobiosisEscherichia colichemistry.chemical_classificationElectron Transport Complex IEthanolbiologyNADH dehydrogenaseGene Expression Regulation BacterialProton PumpsElectron acceptorFumarate reductaseNADElectron transport chainGlycerol-3-phosphate dehydrogenaseBiochemistrychemistryElectron Transport Complex Ibiology.proteinEnergy MetabolismEuropean Journal of Biochemistry
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Detection of mitochondrial electron chain carrier redox status by transhepatic light intensity during rat liver reperfusion.

2003

The aim of the study was to investigate mitochondrial electron transfer during rat liver reperfusion after cold storage and hypothermic machine perfusion. Livers from male Brown Norway rats were preserved (UW) for 10h either by cold storage (CS) or by hypothermic oxygenated perfusion extracorporal (HOPE). Transhepatic photometric analysis allowed determination of the redox status of mitochondrial cytochromes during preservation, rewarming and reperfusion. Mitochondrial electron chain carriers were inhibited at different sites with rotenone and cyanide in some experiments. reversed transcriptional polymerase chain reaction (RT-PCR) was performed after reperfusion concerning transcription of …

AnionsMaleTime FactorsCytochromeLightCold storageCaspase 3ElectronsDNA FragmentationMitochondrionGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundSuperoxidesAnimalsCaspase-9CryopreservationCyanidesbiologySuperoxideCaspase 3Reverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaJNK Mitogen-Activated Protein KinasesTemperatureNADH DehydrogenaseGeneral MedicineRotenoneDNAOrgan PreservationLipid MetabolismCaspase 9MitochondriaRatsCold TemperatureOxygenLight intensitychemistryBiochemistryElectron Transport Chain Complex ProteinsLiverCaspasesReperfusionbiology.proteinCytochromesLipid PeroxidationMitogen-Activated Protein KinasesGeneral Agricultural and Biological SciencesReactive Oxygen SpeciesOxidation-ReductionCryobiology
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DHFR Inhibitors: Reading the Past for Discovering Novel Anticancer Agents.

2019

Dihydrofolate reductase inhibitors are an important class of drugs, as evidenced by their use as antibacterial, antimalarial, antifungal, and anticancer agents. Progress in understanding the biochemical basis of mechanisms responsible for enzyme selectivity and antiproliferative effects has renewed the interest in antifolates for cancer chemotherapy and prompted the medicinal chemistry community to develop novel and selective human DHFR inhibitors, thus leading to a new generation of DHFR inhibitors. This work summarizes the mechanism of action, chemical, and anticancer profile of the DHFR inhibitors discovered in the last six years. New strategies in DHFR drug discovery are also provided, …

AntifungalCancer chemotherapymedicine.drug_classDrug Evaluation Preclinicaldihydrofolate reductase (DHFR) enzymePharmaceutical ScienceAntineoplastic AgentsComputational biologyReview01 natural scienceshybrid compoundsAnalytical Chemistrylcsh:QD241-44103 medical and health sciencesStructure-Activity RelationshipFolic Acidlcsh:Organic chemistryheterocyclic compoundsNeoplasmsDihydrofolate reductaseparasitic diseasesDrug DiscoverymedicineAnimalsHumansPhysical and Theoretical Chemistry030304 developmental biology0303 health sciencesHeterocyclic compoundbiology010405 organic chemistryDrug discoveryOrganic ChemistryDHFR inhibitors as anticancer agentSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciencesDHFR drug discoveryTetrahydrofolate DehydrogenaseMechanism of actionChemistry (miscellaneous)Settore CHIM/03 - Chimica Generale E InorganicaDHFR inhibitors as anticancer agentsbiology.proteinMolecular MedicineFolic Acid Antagonistsmedicine.symptomMolecules (Basel, Switzerland)
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The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen.

1997

A lambda gt11 cDNA library from Candida albicans ATCC 26555 was screened by using pooled sera from two patients with systemic candidiasis and five neutropenic patients with high levels of anti-C. albicans immunoglobulin M antibodies. Seven clones were isolated from 60,000 recombinant phages. The most reactive one contained a 0.9-kb cDNA encoding a polypeptide immunoreactive only with sera from patients with systemic candidiasis. The whole gene was isolated from a genomic library by using the cDNA as a probe. The nucleotide sequence of the coding region showed homology (78 to 79%) to the Saccharomyces cerevisiae TDH1 to TDH3 genes coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH), …

Antigens FungalDNA ComplementaryGenes FungalMolecular Sequence DataBiologyMicrobiologystomatognathic systemCell WallComplementary DNACandida albicansmedicineHumansCloning MolecularCandida albicansFluorescent Antibody Technique IndirectMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseAntibodies FungalAntiserumcDNA libraryCandidiasisAntibodies MonoclonalGlyceraldehyde-3-Phosphate Dehydrogenasesmedicine.diseasebiology.organism_classificationMolecular biologyCorpus albicansBlotting SouthernBiochemistryPolyclonal antibodiesAntigens Surfacebiology.proteinSystemic candidiasisGlycolysisResearch Article
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The Fumarate/Succinate Antiporter DcuB of Escherichia coli Is a Bifunctional Protein with Sites for Regulation of DcuS-dependent Gene Expression

2008

DcuB of Escherichia coli catalyzes C4-dicarboxylate/succinate antiport during growth by fumarate respiration. The expression of genes of fumarate respiration, including the genes for DcuB (dcuB) and fumarate reductase (frdABCD) is transcriptionally activated by C4-dicarboxylates via the DcuS-DcuR two-component system, comprising the sensor kinase DcuS, which contains a periplasmic sensing domain for C4-dicarboxylates. Deletion or inactivation of dcuB caused constitutive expression of DcuS-regulated genes in the absence of C4-dicarboxylates. The effect was specific for DcuB and not observed after inactivation of the homologous DcuA or the more distantly related DcuC transporter. Random and s…

AntiporterMutantlac operonBiologymedicine.disease_causePeptide MappingBiochemistryAntiportersFumaratesEscherichia colimedicineMolecular BiologyEscherichia coliDerepressionDicarboxylic Acid TransportersIon TransportEscherichia coli ProteinsMutagenesisSuccinatesGene Expression Regulation BacterialCell BiologyPeriplasmic spaceFumarate reductaseDNA-Binding ProteinsSuccinate DehydrogenaseAmino Acid SubstitutionBiochemistryGene Knockdown TechniquesMutagenesis Site-DirectedProtein KinasesTranscription FactorsJournal of Biological Chemistry
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Effect of ADH II Deficiency on the Intracellular Redox Homeostasis in Zymomonas mobilis

2011

Mutant strain of the facultatively anaerobic, ethanol-producing bacteriumZymomonas mobilis, deficient in the Fe-containing alcohol dehydrogenase isoenzyme (ADH II), showed impaired homeostasis of the intracellular NAD(P)H during transition from anaerobic to aerobic conditions, and also in steady-state continuous cultures at various oxygen supplies. At the same time, ADH II deficiency in aerobically grown cells was accompanied by a threefold increase of catalase activity and by about 50% increase of hydrogen peroxide excretion. It is concluded that ADH II under aerobic conditions functions to maintain intracellular redox homeostasis and to protect the cells from endogenous hydrogen peroxide.

Article Subjectlcsh:MedicineBiologyZymomonas mobilislcsh:TechnologyGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundOxygen ConsumptionSpecies SpecificityHomeostasisHydrogen peroxidelcsh:ScienceGeneral Environmental ScienceAlcohol dehydrogenaseZymomonaslcsh:Tlcsh:RAlcohol DehydrogenaseHydrogen PeroxideGeneral Medicinebiology.organism_classificationOxygenBiochemistrychemistryCatalasebiology.proteinlcsh:QNAD+ kinaseOxidation-ReductionAnaerobic exerciseNADPHomeostasisIntracellularResearch ArticleThe Scientific World Journal
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Causative role of oxidative stress in a Drosophila model of Friedreich ataxia

2006

Friedreich ataxia (FA), the most common form of hereditary ataxia, is caused by a deficit in the mitochondrial protein frataxin. While several hypotheses have been suggested, frataxin function is not well understood. Oxidative stress has been suggested to play a role in the pathophysiology of FA, but this view has been recently questioned, and its link to frataxin is unclear. Here, we report the use of RNA interference (RNAi) to suppress the Drosophila frataxin gene (fh) expression. This model system parallels the situation in FA patients, namely a moderate systemic reduction of frataxin levels compatible with normal embryonic development. Under these conditions, fh-RNAi flies showed a shor…

AtaxiaBlotting WesternLongevityGene ExpressionCHO Cellsmedicine.disease_causeBiochemistryAconitaseMitochondrial ProteinsCricetulusRNA interferenceCricetinaeIron-Binding ProteinsGeneticsmedicineAnimalsDrosophila ProteinsRNA MessengerMolecular BiologyGeneAconitate HydrataseHyperoxiaGeneticsElectron Transport Complex IbiologyReverse Transcriptase Polymerase Chain ReactionSuccinate dehydrogenasefungiImmunohistochemistryCell biologySuccinate DehydrogenaseOxidative StressDrosophila melanogasterFriedreich AtaxiaFrataxinbiology.proteinRNA Interferencemedicine.symptomOxidative stressBiotechnologyThe FASEB Journal
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Physiology of Zymomonas mobilis: Some Unanswered Questions

2006

The ethanol-producing bacterium Zymomonas mobilis can serve as a model organism for the study of rapid catabolism and inefficient energy conversion in bacteria. Some basic aspects of its physiology still remain poorly understood. Here, the energy-spilling pathways during uncoupled growth, the structure and function of electron transport chain, and the possible reasons for the inefficient oxidative phosphorylation are analysed. Also, the interaction between ethanol synthesis and respiration is considered. The search for mechanisms of futile transmembrane proton cycling, as well as identification of respiratory electron transport complexes, like the energy-coupling NAD(P)H:quinone oxidoreduct…

BiochemistrybiologyCatabolismPhysiologyOxidative phosphorylationNAD+ kinaseQuinone oxidoreductasebiology.organism_classificationNAD(P)H Dehydrogenase (Quinone)Zymomonas mobilisElectron transport chainTransmembrane protein
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