Indirect chelatometric determination of molybdate as lead molybdate
نویسندگان
چکیده
منابع مشابه
The pyrochlore-type molybdate Pr1.37Ca0.63Mo2O7
Praseodymium calcium dimolybdenum hepta-oxide, Pr(1.37)Ca(0.63)Mo(2)O(7), crystallizes in the cubic pyrochlore-type structure. In the crystal structure, MoO(6) octa-hedra are linked together by common corners, forming a three-dimensional [Mo(2)O(6)] network. The Pr and Ca atoms and the remaining O atoms are located in the voids of the [Mo(2)O(6)] network. The Pr and Ca atoms are distributed sta...
متن کاملThe pyrochlore-type molybdate Pr2Mo1.73Sc0.27O7
Dipraseodymium molybdenum scandium hepta-oxide, Pr2Mo1.73Sc0.27O7, crystallizes in the cubic pyrochlore-type structure. In the crystal, (Mo,Sc)O6 octa-hedra are linked together by common corners, forming a three-dimensional [(Mo,Sc)2O6] framework. The Pr atom and another O atom atom are located in the voids of this framework. The Mo and the Sc atom are distributed statistically over the same 16...
متن کاملMolybdate binding by ModA, the periplasmic component of the Escherichia coli mod molybdate transport system.
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...
متن کاملOne- and two-electron reduction of molybdate reversibly bound to the archaeal tungstate/molybdate transporter WtpA.
Reversible binding of the tetrahedral oxoanions MoO(4)(2-) and WO(4)(2-) to two carboxylato ligands of the soluble scavenger protein WtpA from the hyperthermophilic archaeon Pyrococcus furiosus enforces a quasi-octahedral MO(6) coordination in which the +VI oxidation state is destabilized.
متن کاملPhenotypic Restoration by Molybdate of Nitrate
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...
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ژورنال
عنوان ژورنال: BUNSEKI KAGAKU
سال: 1960
ISSN: 0525-1931
DOI: 10.2116/bunsekikagaku.9.172