Granule-derived cationic MPO protein can attach to negatively charged proteins and membrane epitopes of ingested bacteria (Selvaraj RJ et al. 1978; Miyasaki KT et al. 1987). This could be a way of directing HOCl for effective killing (Klebanoff SJ et al. 1999).
MPO is a heme enzyme that uses hydrogen peroxide to oxidize chloride to hypochlorous acid. MPO reacts with hydrogen peroxide, which is produced by stimulated neutrophils, to form the redox intermediate compound I (Winterbourn CC et al 2006; Davies MJ 2011; Pattison DI et al. 2012). Compound I is strongly oxidizing and reacts with a variety of substrates such as halide and pseudo-halide ions to produce hypohalous acids (HOX where X = Cl, Br, SCN). Its main physiological substrate is assumed to be chloride, which undergoes a two-electron oxidation to form hypochlorous acid (HOCl) (Winterbourn CC et al 2006; Davies MJ 2001; Pattison DI et al. 2012).
Hampton, MB, Livesey, JH, Kettle, AJ, Winterbourn, CC
Hawkins, CL, Davies, MJ, Pattison, DI
peroxidase activity of MPO:ferriheme:bacterial cell surface [phagocytic vesicle lumen]
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