Artículos de revistas
Synthesis and electrochemical properties of meldola blue intercalated into barium and calcium phosphates
Registro en:
Sensors And Actuators B-chemical. Elsevier Science Sa, v. 107, n. 1, n. 446, n. 453, 2005.
0925-4005
WOS:000229665700064
10.1016/j.snb.2004.11.002
Autor
Lazarin, AM
Airoldi, C
Institución
Resumen
Meldola blue (MLB) was strongly retained inside the cavity of host layered barium and calcium phosphates, without leaching, and the intercalated compounds were characterized through elemental analysis, X-ray power diffraction (XRD), infrared spectroscopy, scanning electron microscopy, phosphorus nuclear magnetic resonance and electrochemical measurements. The intercalated dye compound was incorporated into a carbon paste electrode and, by means of cyclic voltammetry, its electrochemical properties were investigated. Upon changing the pH of the solution between 2.5 and 7.0, the midpoint potential remained practically constant, giving near -0.020 and -0.019 V versus SCE for barium and calcium phosphates intercalated with MLB. This is not the usual behavior of MLB since its midpoint potential changes considerably in solution phase as the pH is changed. The modified electrodes have proven to be stable and electrocatalytically active for hydrazine oxidation at pH 6.0. (c) 2004 Elsevier B.V. All rights reserved. 107 1 446 453
Ítems relacionados
Mostrando ítems relacionados por Título, autor o materia.
-
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution
Universidade de São Paulo (USP); Univ. Nac. Auton. de México; Universidade Estadual Paulista (Unesp) (1995-12-01)Background: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and ... -
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution
Universidade de São Paulo (USP); Univ. Nac. Auton. de México; Universidade Estadual Paulista (Unesp) (1995-12-01)Background: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and ... -
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution
Oliva, Glaucius; Fontes, Marcos R.M.; Garratt, Richard C.; Altamirano, Myriam M.; Calcagno, Mario L.; Horjales, Eduardo