Cited by 158Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

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Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences

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Ehrenshaft, Marilyn, Deterding, Leesa J., Mason, Ronald P.·2015·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2015.08.003PMC PMC4684788

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Abstract

Proteins comprise a majority of the dry weight of a cell, rendering them a major target for oxidative modification. Oxidation of proteins can result in significant alterations in protein molecular mass such as breakage of the polypeptide backbone and/or polymerization of monomers into dimers, multimers, and sometimes insoluble aggregates. Protein oxidation can also result in structural changes to amino acid residue side chains, conversions that have only a modest effect on protein size but can have widespread consequences for protein function. There are a wide range of rate constants for amino acid reactivity, with cysteine, methionine, tyrosine, phenylalanine, and tryptophan having the highest rate constants with commonly encountered biological oxidants. Free tryptophan and tryptophan protein residues react at a diffusion-limited rate with hydroxyl radical and also have high rate constants for reactions with singlet oxygen and ozone. Although oxidation of proteins in general and tryptophan residues specifically can have effects detrimental to the health of cells and organisms, some modifications are neutral, whereas others contribute to the function of the protein in question or may act as a signal that damaged proteins need to be replaced. This review provides a brief overview of the chemical mechanisms by which tryptophan residues become oxidized, presents both the strengths and the weaknesses of some of the techniques used to detect these oxidative interactions, and discusses selected examples of the biological consequences of tryptophan oxidation in proteins from animals, plants, and microbes.

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Authors: Ehrenshaft, M., Deterding, L. J., & Mason, R. P.
Affiliations: National Institutes of Health (US)
Corresponding author: Ehrenshaft, Marilyn
ORCID: Deterding, Leesa J.
Mason, Ronald P.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2015-12
Volume: 89
Pages: 220-228
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2015.08.003
PMC: PMC4684788
OpenAlex: W2187856084
Cited by: 158
References: 95
Citations by year: 2026: 16 · 2025: 13 · 2024: 15 · 2023: 20 · 2022: 16 · 2021: 22 · 2020: 15 · 2019: 15 · 2018: 14 · 2017: 6 · 2016: 6
FWCI: 0.84
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Environmental Health Sciences
National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords: tryptophan oxidation, protein oxidative modification, reactive oxygen species, hydroxyl radicals, singlet oxygen, ozone, protein aggregation, protein misfolding, protein function
MeSH terms: Animals, Humans, Oxidation-Reduction, Proteins, Mass Spectrometry, Tryptophan, Reactive Oxygen Species

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Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences

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