Redox properties of myeloperoxidase
Open accessAbstract
The heme-containing enzyme myeloperoxidase (MPO) is secreted from polymorphonuclear leukocytes and monocytes. It is involved in host defence and inflammation by oxidation of numerous small molecules. This review summarises our current results on the determination of redox properties of all intermediates involved in the halogenation and peroxidase cycle of MPO. The standard reduction potentials of the redox couples compound I/native MPO, compound I/compound II of MPO, and compound II/native MPO have been determined to be 1.16 V, 1.35 V, and 0.97 V, respectively, at pH 7 and 25 degrees C. Thus, for the first time, a full description of these important thermodynamic parameters of myeloperoxidase has been performed, allowing a better understanding of its extraordinary reactivity.
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MPO is a hemoprotein and its Fe3+/Fe2+ redox states are critical to its role in producing anti-microbial effects.
“MPO is a hemoprotein and its Fe3+/Fe2+ redox states are critical to its role in producing anti-microbial effects (Arnhold et al., 2003).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Arnhold et al., 2003
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- Authors
- Arnhold, J., Furtmüller, P. G., & Obinger, C.
- Affiliations
- Leipzig University (DE)
- BOKU University (AT)
- Venue
- Redox Report
- Publisher
- Informa UK Limited
- Published
- 2003-08
- Volume
- 8
- Issue
- 4
- Pages
- 179-186
- ISSN
- 1351-0002 (ISSN-L)
- 1743-2928
- OpenAlex
- W1986176507
- Cited by
- 91
- References
- 68
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 11 · 2023: 2 · 2022: 8 · 2021: 4 · 2020: 7 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 4 · 2015: 1 · 2013: 4 · 2012: 1
- FWCI
- 0.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Redox Report (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Austrian Science Fund (P 15660)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- myeloperoxidase, redox properties, standard electrode potential, compound I, compound II, heme peroxidase, halogenation, oxidation intermediates
- MeSH terms
- Animals, Binding Sites, Heme, Humans, Peroxidase, Oxidation-Reduction, Molecular Structure
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