Superoxide radicals react with peptide-derived tryptophan radicals with very high rate constants to give hydroperoxides as major products
Abstract
Oxidative damage is a common process in many biological systems and proteins are major targets for damage due to their high abundance and very high rate constants for reaction with many oxidants (both radicals and two-electron species). Tryptophan (Trp) residues on peptides and proteins are a major sink for a large range of biological oxidants as these side-chains have low radical reduction potentials. The resulting Trp-derived indolyl radicals (Trp•) have long lifetimes in some circumstances due to their delocalized structures, and undergo only slow reaction with molecular oxygen, unlike most other biological radicals. In contrast, we have shown previously that Trp• undergo rapid dimerization. In the current study, we show that Trp• also undergo very fast reaction with superoxide radicals, O 2•-, with k 1-2 × 10 9 M-1 s-1. These values do not alter dramatically with peptide structure, but the values of k correlate with overall peptide positive charge, consistent with positive electrostatic interactions. These reactions compete favourably with Trp• dimerization and O 2 addition, indicating that this may be a major fate in some circumstances. The Trp• + O 2•- reactions occur primarily by addition, rather than electron transfer, with this resulting in high yields of Trp-derived hydroperoxides. Subsequent degradation of these species, both stimulated and native decay, gives rise to N-formylkynurenine, kynurenine, alcohols and diols. These data indicate that reaction of O 2•- with Trp• should be considered as a major pathway to Trp degradation on peptides and proteins subjected to oxidative damage.
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Trp• dimerization takes place when O2•− is absent or present at low concentrations.
“Trp• dimerization takes place under conditions where O2•− is absent or present in low concentrations [144].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [144]
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- Authors
- Carroll, L., Pattison, D. I., Davies, J. B., Anderson, R. F., Lopez-Alarcon, C., & Davies, M. J.
- Affiliations
- University of Copenhagen (DK)
- The University of Sydney (AU)
- Australian Nuclear Science and Technology Organisation (AU)
- University of Auckland (NZ)
- Corresponding author
- Davies, Michael J.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2018-04
- Volume
- 118
- Pages
- 126-136
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2793874346
- Cited by
- 48
- References
- 82
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 8 · 2022: 2 · 2021: 5 · 2020: 6 · 2019: 10 · 2018: 2
- FWCI
- 2.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- ResearchSpace (University of Auckland) (submittedVersion)
- Funders
- Australian Research Council (DP140103116)
- Australian Institute of Nuclear Science and Engineering (ALNGRA14021, ALNGRA15521)
- Fondo Nacional de Desarrollo Científico y Tecnológico (1141142)
- Novo Nordisk Fonden (NNF13OC0004294)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Keywords
- tryptophan radical, superoxide, hydroperoxides, tryptophan oxidation, peptide oxidation, rate constants, electrostatic interactions, N-formylkynurenine, kynurenine, oxidative protein damage
- MeSH terms
- Free Radicals, Hydrogen Peroxide, Oxidation-Reduction, Peptides, Superoxides, Tryptophan, Oxidative Stress
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