Heme peroxidases catalyze the hydrogen peroxide-dependent oxidation of a variety of different substrates by means of oxidized Compound I and Compound II intermediates.
Heme peroxidases have a long history and are widely distributed in biological systems. Horseradish peroxidase (HRP), which is one of the most famous members of the family, was first implicated as an oxidizing species in horseradish roots as early as 1810 (Planche 1810) and in the years to follow the colorful spectra of its various reaction intermediates played a key part in the development of rapid kinetics methods (reviewed in Kresge et al. 2004). Entire books have been written on heme peroxidases, exploring their reactivity, properties, and biological function (Everse et al. 1991; Dunford 2010). Peroxidases have been characterized which utilize both c-type hemes (bacterial diheme peroxidases) and redox-active selenocysteine residues (glutathione peroxidases). A...
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