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Lactoperoxidase (LPO, Fe III  in its resting state in the absence of substrates)—an enzyme secreted from human mammary, salivary, and other mucosal glands—catalyzes the oxidation of thiocyanate (SCN − ) by hydrogen peroxide (H 2 O 2 ) to produce hypothiocyanite (OSCN − ), which functions as an antimicrobial agent. The accepted catalytic mechanism, called the halogen cycle, comprises a two-electron oxidation of LPO by H 2 O 2  to produce oxoiron(IV) radicals, followed by O-atom transfer to SCN − . However, the mechanism does not explain biphasic kinetics and inhibition by H 2 O 2  at low concentration of reducing substrate, conditions that may be biologically relevant. We propose an ordered sequential mechanism in which the order of substrate binding is reversed, first SCN −  and then H 2 O 2 . The sequence of substrate binding that is described by the halogen cycle mechanism is actually inhibitory.

Reverse Ordered Sequential Mechanism for Lactoperoxidase with Inhibition by Hydrogen Peroxide