Title : Mechanism of reaction of chlorite with mammalian heme peroxidases.

Pub. Date : 2014 Jun

PMID : 24632343






4 Functional Relationships(s)
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Protein Name
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1 In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range. chlorite myeloperoxidase Homo sapiens
2 In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range. chlorite myeloperoxidase Homo sapiens
3 Chlorite acts as efficient one-electron donor for Compound I and Compound II of MPO and LPO and reacts with the corresponding ferric resting states in a biphasic manner. chlorite myeloperoxidase Homo sapiens
4 The first (rapid) phase is shown to correspond to the formation of a MPO-chlorite high-spin complex, whereas during the second (slower) phase degradation of the prosthetic group was observed. chlorite myeloperoxidase Homo sapiens