نتایج جستجو برای: molybdate phosphomc acid solvent wert oft

تعداد نتایج: 796224  

2003
J. H. GLASER J. A. DEMOSS

ChlD mutants of Escherichia coli are pleiotropic, lacking formate-nitrate reductase activity as well as formate-hydrogenlyase activity. Whole-chain formate-nitrate reductase activity, assayed with formate as the electron donor and measuring the amount of nitrite produced, was restored to wild-type levels in the mutants by addition of 10-4 M molybdate to the growth medium. Under these conditions...

2013
Lilian R. Graser Sophie Jürgens Michael E. Wilhelm Mirza Cokoja Wolfgang A. Herrmann Fritz E. Kühn

Polyoxomolybdates were generated in situ by treating a carboxylic acid-functionalized ionic liquid with an aqueous solution of sodium molybdate. This reaction mixture was applied in the catalytic epoxidation of olefins using hydrogen peroxide as oxidant. The influence of acid and catalyst concentration as well as of the reaction temperature was investigated. The system showed a good performance...

2014
Florian Bittner

In the form of molybdate the transition metal molybdenum is essential for plants as it is required by a number of enzymes that catalyze key reactions in nitrogen assimilation, purine degradation, phytohormone synthesis, and sulfite detoxification. However, molybdate itself is biologically inactive and needs to be complexed by a specific organic pterin in order to serve as a permanently bound pr...

Journal: :Biochimica et biophysica acta 1998
J Imperial M Hadi N K Amy

ModA, the periplasmic-binding protein of the Escherichia coli mod transport system was overexpressed and purified. Binding of molybdate and tungstate to ModA was found to modify the UV absorption and fluorescence emission spectra of the protein. Titration of these changes showed that ModA binds molybdate and tungstate in a 1:1 molar ratio. ModA showed an intrinsic fluorescence emission spectrum...

Journal: :Journal of bacteriology 1975
G T Sperl J A DeMoss

chlD mutants of Escherichia coli lack active nitrate reductase but form normal levels of this enzyme when the medium is supplemented with 10-3 M molybdate. When chlD mutants were grown in unsupplemented medium and then incubated with molybdate in the presence of chloramphenicol, they formed about 5% the normal level of nitrate reductase. Some chlD mutants or the wild type grown in medium supple...

Journal: :Wiener Klinisches Magazin 2021

2007
Shaji Chempath Alexis T. Bell

A theoretical analysis was carried out of the mechanism and kinetics of methane oxidation to formaldehyde occurring on isolated molybdate species supported on silica. Both mono-oxo and di-oxo molybdate structures were used to represent the active centers. The energetics for each elementary reaction was determined from density functional theory calculations, and the entropy changes were determin...

Journal: :Cancer research 1980
C L Bevins N Bashirelahi

In the presence of 10 mM molybdate ion, we are able to detect the appearance of a [6,7-3H]-17,21-dimethyl-19-nor-4,9-pregnadiene-3,20-dione-([3H]R5020) binding moiety in human prostatic cytosol which sedimented at approximately 8S in a glycerol density gradient. The specifically bound [3H]-R5020 was displaced by progesterone, tiramcinolone acetonide, and R5020 but not by cortisol, dihydrotestos...

Journal: :British journal of anaesthesia 1987
A T Sim M D White M A Denborough

The effect of adenylate cyclase activation on the in vitro contractures of control and malignant hyperpyrexia susceptible (MHS) porcine muscle was investigated. While fluoride and molybdate ions potentiated drug-induced contractures in control muscle, other activators of adenylate cyclase (forskolin and noradrenaline) did not. Furthermore, fluoride and molybdate had no effect on MHS skeletal mu...

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