Cited by 198Redox biology and oxidative stressSulfur Compounds in BiologyProtein Structure and Dynamics

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The physiological role of reversible methionine oxidation

Drazic, Adrian, Winter, Jeannette·2014·Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

DOI 10.1016/j.bbapap.2014.01.001

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Abstract

Sulfur-containing amino acids such as cysteine and methionine are particularly vulnerable to oxidation. Oxidation of cysteine and methionine in their free amino acid form renders them unavailable for metabolic processes while their oxidation in the protein-bound state is a common post-translational modification in all organisms and usually alters the function of the protein. In the majority of cases, oxidation causes inactivation of proteins. Yet, an increasing number of examples have been described where reversible cysteine oxidation is part of a sophisticated mechanism to control protein function based on the redox state of the protein. While for methionine the dogma is still that its oxidation inhibits protein function, reversible methionine oxidation is now being recognized as a powerful means of triggering protein activity. This mode of regulation involves oxidation of methionine to methionine sulfoxide leading to activated protein function, and inactivation is accomplished by reduction of methionine sulfoxide back to methionine catalyzed by methionine sulfoxide reductases. Given the similarity to thiol-based redox-regulation of protein function, methionine oxidation is now established as a novel mode of redox-regulation of protein function. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.

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“…sulfoxide reductases (Msrs), particularly mitochondrial MsrB2, reverse methionine oxidation and preserve protein function under oxidative stress (Kim, 2013; Boschi-Muller and Branlant, 2014; Drazic and Winter 2014; Kim et al., 2014; Moskovitz and Smith, 2021; Reyes et al., 2018; Yin et al., 2012).”
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Authors: Drazic, A., & Winter, J.
Affiliations: Center for Integrated Protein Science Munich (DE)
Corresponding author: Winter, Jeannette
ORCID: Drazic, Adrian
Venue: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Publisher: Elsevier BV
Published: 2014-08
Volume: 1844
Issue: 8
Pages: 1367-1382
ISSN: 1570-9639 (ISSN-L)
DOI: 10.1016/j.bbapap.2014.01.001
OpenAlex: W2039213528
Cited by: 198
References: 187
Citations by year: 2026: 8 · 2025: 13 · 2024: 19 · 2023: 11 · 2022: 22 · 2021: 14 · 2020: 15 · 2019: 17 · 2018: 12 · 2017: 18 · 2016: 15 · 2015: 20 · 2014: 13
FWCI: 2.08
Type: journal article
Language: en
Open access: closed
Locations: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: methionine sulfoxide, methionine sulfoxide reductase, post-translational modification, protein inactivation, cysteine oxidation, sulfur-containing amino acids
MeSH terms: Animals, Cell Physiological Phenomena, Humans, Methionine, Oxidation-Reduction, Signal Transduction

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The physiological role of reversible methionine oxidation

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