Peroxidase myelo

Catechol may be oxidized by peroxidases to the reactive intennediate benzo-1,2-quinone, which readily binds to proteins (Bhat et al., 1988) this process, catalysed by rat or human bone-marrow cells in the presence of H2O2 (0.1 mM), is stimulated by phenol (0.1-10 mM), and decreased by hydroquinone and by glutathione, which conjugates with benzo-l,2-quinone. These phenols (phenol, catechol and hydroquinone) may play a role in benzene toxicity to bone marrow all three are formed as benzene metabolites (Smith et al., 1989) and they interact in several ways as far as their bioactivation by (myelo)peroxidases is concerned (Smith et al., 1989 Subrahmanyam et al., 1990). 

Kalf, G, Shurina, R., Renz, J. Schlosser, M. (1990) The role of hepatic metabolites of benzene in bone marrow peroxidase-mediated myelo- and genotoxicity. In Witmer, C.M., Snyder, R.R., Jollow, D.J., Kalf, G.F., Kocsis, J.J. Sipes, I.G., eds, Biological Reactive Intermediates IV, New York, Plenum Press, pp. 443-455... 

Kalf G, Shurina R, Renz J, et al. 1990. The role of hepatic metabolites of benzene in bone marrow peroxidase-mediated myelo- and genotoxicity. Adv Exp Med Biol 283 443-455. 

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