Reactivity of Peroxidase-Derived Oxidants with Proteins, Glycoproteins and Proteoglycans

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The heme peroxidase enzyme family is a major source of reactive oxidants in biological systems. Some of the species formed by these enzymes (e.g. hypochlorous acid, HOCl; hypobromous acid, HOBr; hypothiocyanous acid, HOSCN) appear to be critical components of the innate immune system and play a key role in the killing of invading pathogens (e.g. bacteria, yeasts, fungi parasites) by activated neutrophils and leukocytes. Inadvertent, misplaced or overproduction of these species can however also damage host cells and tissues, and this underlies the strong association between high levels of some of these enzymes and a large number of inflammatory pathologies. Some of the oxidants formed by the enzymes have additional or alternative normal physiological functions, with hypoiodous acid (HOI), formed by thyroid peroxidase being critical to the generation of thyroid hormones, and HOBr formed by peroxidasins playing an important role in the cross-linking of collagen chains in extracellular matrix formation. Proteins, proteoglycans and glycoproteins are major targets for these oxidants both in physiological and pathological situations, as a result of their high abundance and the high rate constants for reaction of some amino acid side-chains with these species, though there are marked differences in the overall rate and selectivity of damage. There is therefore major interest in understanding the kinetics and mechanisms of reaction of these oxidants, the use of some of the products as biomarkers and the biological consequences of these reactions. This review discusses these fields.

Original languageEnglish
Title of host publicationMammalian Heme Peroxidases : Diverse Roles in Health and Disease
PublisherCRC Press
Publication date1 Jan 2021
ISBN (Print)9780367820367
ISBN (Electronic)9781000450613
Publication statusPublished - 1 Jan 2021

Bibliographical note

Publisher Copyright:
© 2022 selection and editorial matter, Clare Hawkins and William M. Nauseef.

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