Cited by 40Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressMetal-Catalyzed Oxygenation Mechanisms

Halogenation Activity of Mammalian Heme Peroxidases

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Arnhold, Jürgen, Malle, Ernst·2022·Antioxidants

Abstract

Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing (pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized (pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation reactions with cell and tissue constituents. The present article reviews basic biochemical and redox mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases. Thyroid peroxidase and peroxidasin are key enzymes for thyroid hormone synthesis and the formation of functional cross-links in collagen IV during basement membrane formation. Special attention is directed to the properties, enzymatic mechanisms, and resulting (pseudo)halogenated products of the immunologically relevant proteins such as myeloperoxidase, eosinophil peroxidase, and lactoperoxidase. The potential role of the (pseudo)halogenated products (hypochlorous acid, hypobromous acid, hypothiocyanite, and cyanate) of these three heme peroxidases is further discussed.

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Crossref · 10.3390/antiox11050890

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  • Myeloperoxidase catalyzes the reaction between H2O2 and Cl− to generate HOCl.

    “Then, the myeloperoxidase enzyme catalyzes the reaction between H2O2 and Cl− to generate HOCl [150], Figure 6.”

    From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [150]

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Authors
Arnhold, J., & Malle, E.
Affiliations
  • Leipzig University (DE)
  • Medical University of Graz (AT)
Corresponding author
  • Arnhold, Jürgen
  • Malle, Ernst
Venue
Antioxidants
Publisher
MDPI AG
Published
2022-04-30
Volume
11
Issue
5
Pages
890
ISSN
2076-3921 (ISSN-L)
OpenAlex
W4225131941
Cited by
40
References
258
Citations by year
2026: 4 · 2025: 11 · 2024: 10 · 2023: 11 · 2022: 3
FWCI
0.92
Type
journal article
Language
en
Open access
Locations
  • Antioxidants (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Qucosa (Saxon State and University Library Dresden) (submittedVersion, cc-by)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
heme peroxidase, halogenation, thyroid peroxidase, peroxidasin, myeloperoxidase, eosinophil peroxidase, lactoperoxidase, thyroid hormone synthesis, basement membrane, hypochlorous acid, hypobromous acid, hypothiocyanite, cyanate, redox mechanism, halide oxidation

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