Dimerization and oxidation of tryptophan in UV-A photolysis sensitized by kynurenic acid

Sormacheva, Ekaterina D.; Sherin, Peter S.; Tsentalovich, Yuri P.

doi:10.1016/j.freeradbiomed.2017.10.007

Cited by 37Photochemistry and Electron Transfer StudiesPhotodynamic Therapy Research StudiesFree Radicals and Antioxidants

Dimerization and oxidation of tryptophan in UV-A photolysis sensitized by kynurenic acid

Sormacheva, Ekaterina D., Sherin, Peter S., Tsentalovich, Yuri P.·2017·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2017.10.007

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Abstract

Photoinduced generation of radicals in the eye lens may play an important role in the modification of proteins leading to their coloration, aggregation, and insolubilization. The radicals can be formed via the reactions of photoexcited endogenous chromophores of the human lens with lens proteins, in particular with tryptophan residues. In the present work we studied the reactions induced by UV-A (315-400nm) light between kynurenic acid (KNA), an effective photosensitizer present in the human lens, and N-acetyl-L-tryptophan (NTrpH) under aerobic and anaerobic conditions. Our results show that the reaction mechanism strongly depends on the presence of oxygen in solution. Under aerobic conditions, the generation of singlet oxygen is the major channel of the effective NTrpH oxidation. In argon-bubbled solutions, the quenching of triplet KNA by NTrpH results in the formation of KNA•- and NTrp• radicals. Under laser pulse irradiation, when the radical concentration is high, the main pathway of the radical decay is the back electron transfer with the restoration of initial reagents. Other reactions include (i) the radical combination yielding NTrp dimers and (ii) the oxygen atom transfer from KNA•- to NTrp• with the formation of oxidized NTrp species and deoxygenated KNA products. In continuous-wave photolysis, even trace amounts of molecular oxygen are sufficient to oxidize the majority of KNA•- radicals with the rate constant of (2.0 ± 0.2) × 10 9 M-1 s-1, leading to the restoration of KNA and the formation of superoxide radical O 2•-. The latter reacts with NTrp• via either the radical combination to form oxidized NTrp (minor pathway), or the electron transfer to restore NTrpH in the ground state (major pathway). As the result, the quantum yields of the starting compound decomposition under continuous-wave anaerobic photolysis are rather low: 1.6% for NTrpH and 0.02% for KNA. The photolysis of KNA with alpha-crystallin yields the same deoxygenated KNA products as the photolysis of KNA with NTrpH, indicating the similarity of the photolysis mechanisms. Thus, inside the eye lens KNA can sensitize both protein photooxidation and protein covalent cross-linking with the minor self-degradation. This may play an important role in the lens protein modifications during the normal aging and cataract development.

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Electron delocalisation on the indole ring causes Trp• radicals to undergo rapid dimerization to Trp-Trp cross-linked species with different C-C and C-N cross-linkages.
“As a consequence of electron delocalisation on the indole ring, Trp• radicals undergo rapid dimerization reactions to give Trp-Trp cross-linked species that produce isomers with different cross-linkages, C-C cross-linked and C-C cross-linked species. C-N [142,143], Figure 55.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [143]

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Authors: Sormacheva, E. D., Sherin, P. S., & Tsentalovich, Y. P.
Affiliations: International Tomography Center (RU)
Novosibirsk State University (RU)
Corresponding author: Sherin, Peter S.
ORCID: Sherin, Peter S.
Tsentalovich, Yuri P.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2017-12
Volume: 113
Pages: 372-384
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2017.10.007
OpenAlex: W2762099131
Cited by: 37
References: 85
Citations by year: 2026: 1 · 2025: 4 · 2024: 1 · 2023: 6 · 2022: 3 · 2021: 9 · 2020: 4 · 2019: 4 · 2018: 5
FWCI: 2.62
Type: journal article
Language: en
Open access: closed
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)
Funders: Grant Council of President of Russian Federation (MK-1515.2017.3)
Russian Foundation for Basic Research (16-33-00669, 17-03-00656)
Complex Program of Basic Research SB RAS (68)
Topics: Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Photodynamic Therapy Research Studies
Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
Keywords: tryptophan, kynurenic acid, light-induced oxidation, singlet oxygen, superoxide, lens proteins, alpha-crystallin, back electron transfer, oxygen atom transfer, photosensitizers, cataract, protein aggregation, quantum yield, aerobic and anaerobic conditions
MeSH terms: Animals, Cattle, Electron Transport, Chemical Fractionation, Kynurenic Acid, Lens, Crystalline, Oxidation-Reduction, Oxygen, Photolysis, Superoxides, Tryptophan, Ultraviolet Rays, Photosensitizing Agents, Dimerization, Singlet Oxygen, alpha-Crystallins

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Dimerization and oxidation of tryptophan in UV-A photolysis sensitized by kynurenic acid

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