SciELO - Scientific Electronic Library Online

 
vol.28 número1Inhibition of the Corrosion of Zinc in 0.01 - 0.04 M H2SO4 by ErythromycinDetermination of Trace Metals by Differential Pulse Voltammetry at Chitosan Modified Electrodes índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados

Revista

Articulo

Indicadores

Links relacionados

  • No hay articulos similaresSimilares en SciELO

Compartir


Portugaliae Electrochimica Acta

versión impresa ISSN 0872-1904

Resumen

TAHBOUB, Yahya R.  y  ABU-SOUD, Husam M.. Steady-State Study of Inhibitory Effect of Nitrite on Myeloperoxidase Catalytic Activity by Hydrogen Peroxide Biosensor. Port. Electrochim. Acta [online]. 2010, vol.28, n.1, pp.27-38. ISSN 0872-1904.

Myeloperoxidase (MPO) is a neutrophil enzyme that employs hydrogen peroxide (H2O2) to catalyze the oxidation of halides and thiocyanate to their respective hypohalous acids. In this study, the inhibitory effect of nitrite (NO2-) on MPO-catalytic activity was investigated electrochemically. H2O2 consumption during steady-state catalysis was monitored amperometrically by a carbon fiber based H2O2-biosensor at 25 oC. Optimized initial concentrations were 50 nM MPO, 10 μM H2O2, and a selected halide or thiocyanate concentration from physiological range. Under these conditions, reactions were monophasic and rapid (complete H2O2 consumption occurs in < 10 s). As concentration of NO2- increases, reactions change to biphasic (rapid step followed by a slow step) and both steps have been inhibited by NO2-. Our results confirmed the inhibitory effect of NO2- and demonstrated for the first time that NO2- is a strong inhibitor towards MPO-catalyzed oxidation of iodide and bromide; and a weak inhibitor towards MPO-catalyzed oxidation of chloride and thiocyanate.

Palabras clave : nitric oxide; nitrite; myeloperoxidase; catalytic activity; H2O2-biosensor.

        · texto en Inglés     · Inglés ( pdf )

 

Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons