Protein oxidation and peroxidation

By M. Davies. Biochemical Journal, 2016

767 citations recorded by the source corpus.

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.

Subfields: Clinical Biochemistry, Inorganic Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/245e1ceca1b56e3e065908177526e658f5410dbf

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In Clinical Biochemistry

1. I. Peluso
2. F. Altieri
3. Ilaria Marrocco

In Molecular Biology

1. Karl-Josef Dietz
2. I. Peluso
3. F. Altieri
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Citations in the corpus

• Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans (2017, background): “Several amino acidic residues can undergo oxidative modifications including oxidation of sulphur-containing residues, hydroxylation of aromatic and aliphatic groups, nitration of tyrosine residues, nitrosylation and glutathionylation of cysteine residues, chlorination of aromatic groups and primary ”
• Antioxidant response mechanism of freshwater microalgae species to reactive oxygen species production: a mini review (2020, background): “ROS have also been shown to be detrimental to freshwater microalgae lipids and proteins leading to the modification of peptide chain and amino acid [15], disruption of enzyme and ATP production and subsequently”
• The Role of the Plant Antioxidant System in Drought Tolerance (2019, background): “Within proteins, the thiol groups of both cysteine (Cys) and methionine (Met) are the major sites of oxidative post-translational modifications (PTMs) [90].”