Search results for "vanA"
showing 10 items of 345 documents
CCDC 1855149: Experimental Crystal Structure Determination
2019
Related Article: Pasi Salonen, Anssi Peuronen, Jari Sinkkonen, Ari Lehtonen|2019|Inorg.Chim.Acta|489|108|doi:10.1016/j.ica.2019.02.011
CCDC 802518: Experimental Crystal Structure Determination
2011
Related Article: O.Wichmann, H.Sopo, A.Lehtonen, R.Sillanpaa|2011|Eur.J.Inorg.Chem.||1283|doi:10.1002/ejic.201001251
CCDC 802523: Experimental Crystal Structure Determination
2011
Related Article: O.Wichmann, H.Sopo, A.Lehtonen, R.Sillanpaa|2011|Eur.J.Inorg.Chem.||1283|doi:10.1002/ejic.201001251
CCDC 1569236: Experimental Crystal Structure Determination
2017
Related Article: Pasi Salonen, Anssi Peuronen, Ari Lehtonen|2017|Inorg.Chem.Commun.|86|165|doi:10.1016/j.inoche.2017.10.017
CCDC 261263: Experimental Crystal Structure Determination
2006
Related Article: Zhenyu Shi, Jun Peng, C.J.Gomez-Garcia, S.Benmansour, Xiaojun Gu|2006|J.Solid State Chem.|179|253|doi:10.1016/j.jssc.2005.09.051
Controlled thermal oxidation of nanostructured vanadium thin films
2016
Abstract Pure V thin films were dc sputtered with different pressures (0.4 and 0.6 Pa) and particle incident angles α of 0°, 20° and 85°, by using the GLancing Angle Deposition (GLAD) technique. The sputtered films were characterized regarding their electrical resistivity behaviour in atmospheric pressure and in-vacuum conditions as a function of temperature (40–550 °C), in order to control the oxidation process. Aiming at comprehending the oxidation behaviour of the samples, extensive morphological and structural studies were performed on the as-deposited and annealed samples. Main results show that, in opposition to annealing in air, the columnar nanostructures are preserved in vacuum con…
Oxidovanadium(V) amine bisphenolates as epoxidation, sulfoxidation and catechol oxidation catalysts
2017
Air-stable oxidovanadium(V) complexes with tetradentate amine bisphenolate ligands were made by the reaction of VOSO4·xH2O and ligand precursors in MeOH solutions. Isolated compounds were studied as catechol oxidase models as well as catalysts for epoxidation and sulfoxidation reactions. All compounds can catalyse such oxidation reactions without notable structure-activity correlations. The 51V NMR studies indicate that the complexes turn to the number of different species during the catalytic experiments. peerReviewed
Phosphorylated intermediate of a transport ATPase and activity of protein kinase in membranes from corn roots
1983
A maize-root microsomal fraction was enriched in ATPase by treatment with Triton X-100. This activity, which reached 1.2-2.0/mumol Pi x min-1 x mg protein-1, was specific for ATP, very slightly stimulated by K+, inhibited by orthovanadate and diethylstilbestrol, resistant to oligomycin and azide, and had a Km of 1.2 mM MgATP. Incubation of the microsomal fraction with [gamma 32-P]ATP followed by electrophoresis in acid conditions revealed the presence of several phosphoproteins. The phosphorylation of a 110000-Mr polypeptide reached the steady-state level in less than 5 s and rapidly turned over the phosphate group. The phosphorylation level was an hyperbolic function of the [ATP] with a Km…
Inhibition of adenosine trephosphatase activity from a plasma membrane fraction of acer pseudoplatanus cells by 2,2,2-trichloroethyl 3,4-dichlorocarb…
1986
2,2,2-Trichloroethyl 3,4-dichlorocarbanilate (SW26) is toxic for Acer pseudoplatanus cell cultures. It inhibited the cellular proton extrusion and depolarized the plasmalemma. In vitro, it inhibited the plasma membrane ATPase. SW 26 was also inhibitory to membrane ATPases of other origins-plant (maize shoot), fungus (Schizosaccharomyces pombe), and animal (dog kidney)-with about the same efficiency (7.5 micromolar < I(50) < 22 micromolar). It did not inhibit the oligomycin-sensitive ATPase from purified plant mitochondria, nor molybdate-sensitive soluble phosphatases. SW26 was more specific for plasma membrane ATPases than diethylstilbestrol or vanadate. A Lineweaver-Burk plot analysis show…
Cercospora beticola Toxin Inhibits Vanadate-Sensitive H+ Transport in Corn Root Membrane Vesicles
1988
The effect of Cercospora beticola toxin on the transport of protons by vanadate-sensitive ATPase was studied with corn (Zea mays) root microsomal vesicles prepared by differential centrifugation, sedimentation through a sucrose cushion, and washing with Triton X-100 plus KBr. In these preparations, addition of ATP induced intravesicular H(+)-accumulation as evidenced by a rapid quenching of the fluorescence of 9-amino-6-chloro-2-methoxy acridine. This quenching was relatively unaffected by inhibitors of mitochondrial and tonoplast-type ATPases, but was strongly reduced by inhibitors of plasma membrane H(+)-ATPase. C. beticola toxin markedly inhibited ATP dependent H(+)-transport, and this e…