Oxidation of methionyl residues in proteins: Tools, targets, and reversal
Abstract
Methionine (Met) is one of the most readily oxidized amino acid constituents of proteins. It is attacked by H2O2, hydroxyl radicals, hypochlorite, chloramines, and peroxynitrite, all these oxidants being produced in biological systems. The oxidation product, Met sulfoxide, can be reduced back to Met by Met sulfoxide reductase. Numerous proteins lose functional activity by Met oxidation. However, functional activation of proteins by Met oxidation has also been observed. Functional changes by Met oxidation in a given protein appear to have pathophysiological significance in some cases. Considering the reversibility of Met oxidation and the functional changes associated with the oxidation, it seems possible that Met oxidation/reduction in proteins may be one means to control homeostasis in biological systems.
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Methionine is reversibly oxidized to methionine sulfoxide and irreversibly oxidized to methionine sulfone; methionine sulfone is stable and not targeted by methionine sulfoxide reductases.
“In contrast to the non-enzymatic oxidation of methionine to methionine sulfoxide, the reduction is catalyzed by methionine sulfoxide reductases [20]. Further oxidation results in methionine sulfone formation, which is not targeted by methionine sulfoxide reductases and has to be considered as a stable modification [21].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [20]
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- Authors
- Vogt, W.
- Affiliations
- Max Planck Institute of Experimental Medicine (DE)
- Corresponding author
- Vogt, Walther
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 1995-01
- Volume
- 18
- Issue
- 1
- Pages
- 93-105
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2037116841
- Cited by
- 883
- References
- 0
- Citations by year
- 2026: 11 · 2025: 19 · 2024: 14 · 2023: 18 · 2022: 24 · 2021: 36 · 2020: 21 · 2019: 24 · 2018: 32 · 2017: 40 · 2016: 33 · 2015: 38 · 2014: 40 · 2013: 42 · 2012: 43
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- methionine oxidation, protein oxidation, methionine sulfoxide, methionine sulfoxide reductase, protein reactivation, oxidative stress, peroxynitrite, hydroxyl radicals, hypochlorite, chloramines, hydrogen peroxide, proteostasis
- MeSH terms
- alpha 1-Antitrypsin, Complement C5, Free Radicals, Hormones, Humans, Methionine, Oxidation-Reduction, Oxidoreductases, Proteins, Methionine Sulfoxide Reductases
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