Search results for "NADH dehydrogenase"

showing 5 items of 25 documents

Conflicting molecular phylogenies of European long-eared bats (Plecotus) can be explained by cryptic diversity

2002

Abstract Conflicting phylogenetic signals of two data sets that analyse different portions of the same molecule are unexpected and require an explanation. In the present paper we test whether (i) differential evolution of two mitochondrial genes or (ii) cryptic diversity can better explain conflicting results of two recently published molecular phylogenies on the same set of species of long-eared bats (genus Plecotus). We sequenced 1714 bp of three mitochondrial regions (16S, ND1, and D-loop) of 35 Plecotus populations from 10 European countries. A likelihood ratio test revealed congruent phylogenetic signals of the three data partitions. Our phylogenetic analyses demonstrated that the exis…

Polymorphism GeneticTime FactorsGeographyPhylogenetic treeLineage (evolution)Plecotus macrobullarisZoologyNADH DehydrogenaseSequence Analysis DNABiologybiology.organism_classificationEvolution MolecularPhylogeneticsChiropteraRNA Ribosomal 16SGeneticsAnimalsInsect ProteinsPlecotus auritusPlecotusMolecular clockMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsPlecotus austriacusMolecular Phylogenetics and Evolution
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First Data on the Molecular Phylogeography of Scincid Lizards of the Genus Mabuya

2000

A 487-bp fragment of the mitochondrial 16S rRNA gene was sequenced in 26 species of the circumtropical lizard genus Mabuya and used to analyze phylogenetic relationships within the genus. The species from Africa and Madagascar formed a monophyletic group relative to the included Asian and South American taxa. The Malagasy species included (M. elegans, M. cf. dumasi, and M. comorensis) did not appear as a monophylum. Combined and separate analysis of the 16S data and additional sequences of the mitochondrial 12S rRNA, ND4, and cytochrome b genes (a total of 2255 bp) in one Asian, two Malagasy, and two African species also did not result consistently in a monophyletic grouping of the Malagasy…

RNA MitochondrialMabuyaZoologyMonophylyGenusRNA Ribosomal 16Sbiology.animalMadagascarGeneticsAnimalsMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsbiologyPhylogenetic treeLizardCytochrome bLizardsNADH DehydrogenaseEmigration and ImmigrationCytochrome b Groupbiology.organism_classificationBiological EvolutionPhylogeographyTaxonRNA RibosomalAfricaRNAMolecular Phylogenetics and Evolution
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NADH dehydrogenase deficiency results in low respiration rate and improved aerobic growth of Zymomonas mobilis.

2008

The respiratory chain of the ethanol-producing bacterium Zymomonas mobilis is able to oxidize both species of nicotinamide cofactors, NADH and NADPH. A mutant strain with a chloramphenicol-resistance determinant inserted in ndh (encoding an NADH : CoQ oxidoreductase of type II) lacked the membrane NADH and NADPH oxidase activities, while its respiratory d-lactate oxidase activity was increased. Cells of the mutant strain showed a very low respiration rate with glucose and no respiration with ethanol. The aerobic growth rate of the mutant was elevated; exponential growth persisted longer, resulting in higher biomass densities. For the parent strain a similar effect of aerobic growth stimulat…

Respiratory chainDehydrogenaseAcetaldehydeMicrobiologyZymomonas mobilisMixed Function Oxygenaseschemistry.chemical_compoundBacterial ProteinsOxidoreductaseRespirationBiomasschemistry.chemical_classificationOxidase testZymomonasbiologyEthanolCell MembraneAcetaldehydeNADH Dehydrogenasebiology.organism_classificationNADAerobiosisOxygenMutagenesis InsertionalGlucosechemistryBiochemistryRespiration rateOxidation-ReductionGene DeletionNADPMicrobiology (Reading, England)
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Natural substances (acetogenins) from the family Annonaceae are powerful inhibitors of mitochondrial NADH dehydrogenase (Complex I).

1994

Natural products from the plants of the family Annonaceae, collectively called Annonaceous acetogenins, are very potent inhibitors of the NADH-ubiquinone reductase (Complex I) activity of mammalian mitochondria. The properties of five of such acetogenins are compared with those of rotenone and piericidin, classical potent inhibitors of Complex I. Rolliniastatin-1 and rolliniastatin-2 are more powerful than piericidin in terms of both their inhibitory constant and the protein-dependence of their titre in bovine submitochondrial particles. These acetogenins could be considered therefore the most potent inhibitors of mammalian Complex I. Squamocin and otivarin also have an inhibitory constant …

StereochemistryPyridinesSubmitochondrial ParticlesAnnonacinRespiratory chainIn Vitro TechniquesBiochemistryMitochondria Heartchemistry.chemical_compoundRotenoneAnimalsNADH NADPH OxidoreductasesSubmitochondrial particleFuransMolecular BiologyNADH dehydrogenase complexchemistry.chemical_classificationElectron Transport Complex IPlants MedicinalbiologyMolecular StructureCell BiologyRotenonebiology.organism_classificationEnzymechemistryBiochemistryAnnonaceaeCattleBullatacinResearch Article
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Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase

2001

The membrane fraction of Bacillus subtilis catalyzes the reduction of fumarate to succinate by NADH. The activity is inhibited by low concentrations of 2-(heptyl)-4-hydroxyquinoline-N-oxide (HOQNO), an inhibitor of succinate: quinone reductase. In sdh or aro mutant strains, which lack succinate dehydrogenase or menaquinone, respectively, the activity of fumarate reduction by NADH was missing. In resting cells fumarate reduction required glycerol or glucose as the electron donor, which presumably supply NADH for fumarate reduction. Thus in the bacteria, fumarate reduction by NADH is catalyzed by an electron transport chain consisting of NADH dehydrogenase (NADH:menaquinone reductase), menaqu…

biologyATP synthaseBiochemistryChemistryProtonophoreSuccinate dehydrogenaseNADH dehydrogenasebiology.proteinReductaseFumarate reductaseBiochemistryRedoxElectron transport chainEuropean Journal of Biochemistry
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