Halogenation Activity of Mammalian Heme Peroxidases
Open accessAbstract
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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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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Detoxification of Selenite to Form Selenocyanate in Mammalian Cells
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Chuang, C. Y., Degendorfer, G., Hammer, A., Whitelock, J. M., Malle, E., & Davies, M. J. (2014) · Biochemical Journal · doi:10.1042/bj20131471 · Cited by 39 · see citing works
Self-citation
Flagged first, then by citations
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The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works
- 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)
- PMC
- PMC9138014
- 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
- gold
- doi.org
- Licence
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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