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Cited by 952Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Protein oxidation and peroxidation

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Davies, Michael J.·2016·Biochemical Journal
DOI 10.1042/bj20151227PMC PMC4819570
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Abstract

Proteins are major targets for radicals and two-electron oxidants in biological systems due to their abundance and high rate constants for reaction. With highly reactive radicals damage occurs at multiple side-chain and backbone sites. Less reactive species show greater selectivity with regard to the residues targeted and their spatial location. Modification can result in increased side-chain hydrophilicity, side-chain and backbone fragmentation, aggregation via covalent cross-linking or hydrophobic interactions, protein unfolding and altered conformation, altered interactions with biological partners and modified turnover. In the presence of O2, high yields of peroxyl radicals and peroxides (protein peroxidation) are formed; the latter account for up to 70% of the initial oxidant flux. Protein peroxides can oxidize both proteins and other targets. One-electron reduction results in additional radicals and chain reactions with alcohols and carbonyls as major products; the latter are commonly used markers of protein damage. Direct oxidation of cysteine (and less commonly) methionine residues is a major reaction; this is typically faster than with H2O2, and results in altered protein activity and function. Unlike H2O2, which is rapidly removed by protective enzymes, protein peroxides are only slowly removed, and catabolism is a major fate. Although turnover of modified proteins by proteasomal and lysosomal enzymes, and other proteases (e.g. mitochondrial Lon), can be efficient, protein hydroperoxides inhibit these pathways and this may contribute to the accumulation of modified proteins in cells. Available evidence supports an association between protein oxidation and multiple human pathologies, but whether this link is causal remains to be established.

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  • Highly reactive species damage numerous sites at side-chains and backbones of proteins, while less reactive species have higher selectivity regarding targeted residues.

    “Highly reactive species damage numerous sites at side-chains and backbones of proteins, while less reactive species have higher selectivity regarding targeted residues [7].”

    From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [7]

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Authors
Davies, M. J.
Affiliations
University of Copenhagen (DK)
Corresponding author
Davies, Michael J.
ORCID
Davies, Michael J.
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2016-03-29
Volume
473
Issue
7
Pages
805-825
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bj20151227
PMC
PMC4819570
OpenAlex
W2318905955
Cited by
952
References
14
Citations by year
2026: 89 · 2025: 93 · 2024: 79 · 2023: 102 · 2022: 77 · 2021: 124 · 2020: 121 · 2019: 109 · 2018: 73 · 2017: 67 · 2016: 18
FWCI
8.08
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochemical Journal (publishedVersion, other-oa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
Funders
  • Novo Nordisk (NNF13OC0004294)
  • Novo Nordisk Fonden (NNF13OC0004294)
  • Australian Research Council (DP160102063, DP140103116, CE0561607)
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
protein oxidation, protein peroxidation, peroxy radicals, protein damage, cysteine oxidation, methionine oxidation, protein aggregation, protein unfolding, protein turnover, proteasome, lysosomes, Lon protease, oxidative stress, human disease
MeSH terms
Animals, Cysteine, Humans, Hydrogen Peroxide, Lysosomes, Methionine, Oxidation-Reduction, Oxygen, Protein Processing, Post-Translational, Proteasome Endopeptidase Complex, Hydrophobic and Hydrophilic Interactions, Proteolysis

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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.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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