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Heme-dependent haloperoxidases

Heme-dependent haloperoxidases generate HOX as reactive species from H2O2 and X, which represents an X+ equivalent capable of undergoing electrophilic addition at electron-rich centers [270,271]. Aprototype biocatalyst of this group is the chloroperoxidase from Caldariomyces Jumago [272]. In many natural systems, such enzymes are responsible for the halogenation of electron-rich aromatic cores. [Pg.263]

For electron-rich substrates, nature often uses flavin-dependent halogenases (e.g. chlorotetracycline), vanadium haloperoxidases (snyderol, Figure 7.4) or heme-iron haloperoxidases (tetraiodothyronine. Figure 7.4) for this role (Figure 7.5). For electron-deficient molecules such as alkanes, mononuclear iron... [Pg.147]

The haloperoxidases are a class of enzymes that catalyze the oxidation of halides via a reactive peroxometal active site. These enzymes are named according to the most electronegative halide they are able to oxidize. Hence, a bromoperoxidase can oxidize bromide and iodide but not chloride, whereas a chloroperoxidase can oxidize all three. Haloperoxidases are found in most living organisms and predominately fall into two classes the iron heme-based and vanadium-dependent enzymes. Of these, heme-based enzymes are found in mammals, where they provide a vital... [Pg.160]


See other pages where Heme-dependent haloperoxidases is mentioned: [Pg.27]    [Pg.1383]    [Pg.1384]    [Pg.27]    [Pg.1383]    [Pg.1384]    [Pg.148]    [Pg.1383]    [Pg.208]    [Pg.303]    [Pg.758]    [Pg.5460]    [Pg.5459]    [Pg.1383]    [Pg.1383]   


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Haloperoxidases

Heme-haloperoxidase

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