Search results for "Protonophore"

showing 4 items of 4 documents

The Plant Inorganic Pyrophosphatase Does Not Transport K+ in Vacuole Membrane Vesicles Multilabeled with Fluorescent Probes for H+, K+, and Membrane …

1995

Abstract It has been claimed that the inorganic pyrophosphatase (PPase) of the plant vacuolar membrane transports K+ in addition to H+ in intact vacuoles (Davies, J. M., Poole, R. J., Rea, P. A., and Sanders, D.(1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11701-11705). Since this was not confirmed using the purified and reconstituted PPase consisting of a 75-kDa polypeptide (Sato, M. H., Kasahara, M., Ishii, N., Homareda, H., Matsui, H., and Yoshida, M. (1994) J. Biol. Chem. 269, 6725-6728), these authors proposed that K+ transport by the PPase is dependent on its association with other membrane components lost during purification. We have examined the hypothesis of K+ translocation by the PP…

0106 biological sciencespyrophosphataseProtonophoreIonophoreVacuole01 natural sciencesBiochemistryPyrophosphateMembrane Potentials03 medical and health scienceschemistry.chemical_compoundValinomycinvitis viniferahydrolyseion potassiumtransport membranaire[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]PyrophosphatasesMolecular BiologyComputingMilieux_MISCELLANEOUSFluorescent Dyes030304 developmental biologyionophoreMembrane potential0303 health sciencesInorganic pyrophosphatasemembrane vacuolaireIon TransportVesicleIntracellular MembranesCell BiologyPlantsEnzyme ActivationInorganic PyrophosphataseBiochemistrychemistrypotentiel membranaireVacuolesPotassiumBiophysicsProtonsvigneHydrogen010606 plant biology & botanyJournal of Biological Chemistry
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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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The effect of amphiphilic compounds on the secretion of levansucrase by Zymomonas mobilis

2005

Abstract The effect of some aliphatic (n-butanol to n-hexadecanol) and aromatic (benzyl and phenethyl alcohols), anesthetics (procaine) and surfactants (Tween 20 to Tween 80) on the secretion of levansucrase by the levan-producing strain of Gram-negative ethanologenic bacteria Zymomonas mobilis 113S were examined in this study. During incubation of Z. mobilis cells with sucrose (10 mM) a decrease of the levansucrase activity was observed in the presence of these amphiphilic compounds concomitantly with an increase of a total amount of protein in the medium. Since none of the compounds under study had any effect on enzyme activity in vitro observed structure- and concentration-dependent rela…

biologyChemiosmosisProtonophoreLevansucrase activityATPaseLevansucraseBioengineeringbiology.organism_classificationApplied Microbiology and BiotechnologyBiochemistryZymomonas mobilischemistry.chemical_compoundBiochemistrychemistrybiology.proteinSodium azideSecretionProcess Biochemistry
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Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate:menaquinone oxidoreductase from the Gram-positiv…

2006

In Gram-positive bacteria and other prokaryotes containing succinate:menaquinone reductases, it has previously been shown that the succinate oxidase and succinate:menaquinone reductase activities are lost when the transmembrane electrochemical proton potential, Deltap, is abolished by the rupture of the bacteria or by the addition of a protonophore. It has been proposed that the endergonic reduction of menaquinone by succinate is driven by the electrochemical proton potential. Opposite sides of the cytoplasmic membrane were envisaged to be separately involved in the binding of protons upon the reduction of menaquinone and their release upon succinate oxidation, with the two reactions linked…

chemistry.chemical_classificationbiologyProtonophoreChemiosmosisSuccinic AcidProton-Motive ForceBacillusVitamin K 2HemeReductasebiology.organism_classificationBiochemistryRedoxCatalysisSuccinate DehydrogenaseEnzymeBiochemistrychemistryBacterial ProteinsFumaratesOxidoreductaseBacillus licheniformisOxidoreductasesOxidation-ReductionBacteriaBiochemistry
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