Steady-State Study of Inhibitory Effect of Nitrite on Myeloperoxidase Catalytic Activity by Hydrogen Peroxide Biosensor

• Autor(a) principal: Tahboub,Yahya R.
• Data de Publicação: 2010
• Outros Autores: Abu-Soud,Husam M.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
• Texto Completo: http://scielo.pt/scielo.php?script=sci_arttext&pid=S0872-19042010000100003
• topic: nitric oxide; nitrite; myeloperoxidase; catalytic activity; H2O2-biosensor

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.