Hydroxyl‐radical production in physiological reactions: A novel function of peroxidase
Abstract
Peroxidases catalyze the dehydrogenation by hydrogen peroxide (H2O2) of various phenolic and endiolic substrates in a peroxidatic reaction cycle. In addition, these enzymes exhibit an oxidase activity mediating the reduction of O2 to superoxide (O2.-) and H2O2 by substrates such as NADH or dihydroxyfumarate. Here we show that horseradish peroxidase can also catalyze a third type of reaction that results in the production of hydroxyl radicals (.OH) from H2O2 in the presence of O2.-. We provide evidence that to mediate this reaction, the ferric form of horseradish peroxidase must be converted by O2.- into the perferryl form (Compound III), in which the haem iron can assume the ferrous state. It is concluded that the ferric/perferryl peroxidase couple constitutes an effective biochemical catalyst for the production of .OH from O2.- and H2O2 (iron-catalyzed Haber-Weiss reaction). This reaction can be measured either by the hydroxylation of benzoate or the degradation of deoxyribose. O2.- and H2O2 can be produced by the oxidase reaction of horseradish peroxidase in the presence of NADH. The .OH-producing activity of horseradish peroxidase can be inhibited by inactivators of haem iron or by various O2.- and .OH scavengers. On an equimolar Fe basis, horseradish peroxidase is 1-2 orders of magnitude more active than Fe-EDTA, an inorganic catalyst of the Haber-Weiss reaction. Particularly high .OH-producing activity was found in the alkaline horseradish peroxidase isoforms and in a ligninase-type fungal peroxidase, whereas lactoperoxidase and soybean peroxidase were less active, and myeloperoxidase was inactive. Operating in the .OH-producing mode, peroxidases may be responsible for numerous destructive and toxic effects of activated oxygen reported previously.
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Phagocytosis of bacteria during inflammation is accompanied by increased oxygen consumption resulting in formation of superoxide anion radical.
“Phagocytosis of bacteria, which occurs during inflammation, is accompanied by a dramatic increase in oxygen consumption resulting in the formation of superoxide anion radical (O2•-) which is quickly converted to hydrogen peroxide (H2O2), spontaneously, or by the enzyme superoxide dismutase.”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [21]
Hydrogen peroxide can oxidise halide ions to hypochlorous acid, which can react with amines to produce chloramines, some of which are very toxic.
“Peroxide hydrogen can also oxidise halide ions (Cl-) to hypochlorous acid (HOCl), which is a strong oxidant that can react with amines producing chloramines, some of them being very toxic [18,19,20,21,22].”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [21]
Essential oils may possess anti-inflammatory activities of interest in food, cosmetic, and human health.
“Essential oils are complex mixtures isolated from aromatic plants which may possess antioxidant and anti-inflammatory activities of interest in thye food and cosmetic industries as well as in the human health field.”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [21]
Hydrogen peroxide can be reduced by transition metal ions to generate hydroxyl radical, which can react with polyunsaturated fatty acids to produce peroxyl radicals.
“Hydrogen peroxide can then also be reduced by transition metal ions generating the hydroxyl radical (HO°), one of the strongest oxidizing agents that can rapidly react with polyunsaturated fatty acids, resulting the production of peroxyl radicals (ROO•).”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [21]
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- Authors
- Chen, S., & Schopfer, P.
- Affiliations
- University of Freiburg (DE)
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1999-03-05
- Volume
- 260
- Issue
- 3
- Pages
- 726-735
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1556055954
- Cited by
- 449
- References
- 51
- Citations by year
- 2026: 5 · 2025: 15 · 2024: 7 · 2023: 16 · 2022: 24 · 2021: 14 · 2020: 14 · 2019: 20 · 2018: 18 · 2017: 22 · 2016: 34 · 2015: 23 · 2014: 25 · 2013: 15 · 2012: 20
- FWCI
- 4.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- hydroxyl radical generation, horseradish peroxidase, superoxide, hydrogen peroxide, compound III, Haber-Weiss reaction, iron-catalyzed oxidation, haem iron, NADH oxidation, lactoperoxidase, soybean peroxidase, myeloperoxidase, deoxyribose degradation, reactive oxygen species, peroxidase isoforms
- MeSH terms
- Enzyme Inhibitors, Horseradish Peroxidase, Hydrogen Peroxide, Superoxides, Hydroxyl Radical
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