Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation

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Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation. / Ignasiak, Marta; Frackowiak, Kamil; Pedzinski, Tomasz; Davies, Michael J.; Marciniak, Bronisław.

In: Free Radical Biology and Medicine, Vol. 153, 2020, p. 12-16.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Ignasiak, M, Frackowiak, K, Pedzinski, T, Davies, MJ & Marciniak, B 2020, 'Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation', Free Radical Biology and Medicine, vol. 153, pp. 12-16. https://doi.org/10.1016/j.freeradbiomed.2020.03.022

APA

Ignasiak, M., Frackowiak, K., Pedzinski, T., Davies, M. J., & Marciniak, B. (2020). Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation. Free Radical Biology and Medicine, 153, 12-16. https://doi.org/10.1016/j.freeradbiomed.2020.03.022

Vancouver

Ignasiak M, Frackowiak K, Pedzinski T, Davies MJ, Marciniak B. Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation. Free Radical Biology and Medicine. 2020;153:12-16. https://doi.org/10.1016/j.freeradbiomed.2020.03.022

Author

Ignasiak, Marta ; Frackowiak, Kamil ; Pedzinski, Tomasz ; Davies, Michael J. ; Marciniak, Bronisław. / Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation. In: Free Radical Biology and Medicine. 2020 ; Vol. 153. pp. 12-16.

Bibtex

@article{e51a1329b8bf4ef298d93b21c6a2b088,
title = "Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation",
abstract = "Tyrosine residues (Tyr) on proteins are a favoured site of one-electron oxidation due to their low one-electron reduction potentials. In this work, light-induced oxidation of Tyr residues was investigated using direct ionisation (via 266 nm light excitation) and sensitized photo-oxidation (by 3-carboxybenzophenone as sensitizer and 355 nm). Light emission (fluorescence) was observed at 410–440 nm as a result of Tyr oxidation. This novel light emission process is shown to be dependent on the solvent and aromatic ring substituents, however it does not depend on pH. It is proposed, that after initial formation of tyrosine phenoxyl radicals (TyrO●) by one electron-oxidation, the TyrO● absorbs a second photon to give an excited state species that undergoes subsequent light emission. The intensity of this emission depends on the Tyr concentration, and the detection of this emission can be used to identify and quantify one-electron formation of oxidized Tyr residues on proteins.",
author = "Marta Ignasiak and Kamil Frackowiak and Tomasz Pedzinski and Davies, {Michael J.} and Bronisław Marciniak",
year = "2020",
doi = "10.1016/j.freeradbiomed.2020.03.022",
language = "English",
volume = "153",
pages = "12--16",
journal = "Free Radical Biology & Medicine",
issn = "0891-5849",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Unexpected light emission from tyrosyl radicals as a probe for tyrosine oxidation

AU - Ignasiak, Marta

AU - Frackowiak, Kamil

AU - Pedzinski, Tomasz

AU - Davies, Michael J.

AU - Marciniak, Bronisław

PY - 2020

Y1 - 2020

N2 - Tyrosine residues (Tyr) on proteins are a favoured site of one-electron oxidation due to their low one-electron reduction potentials. In this work, light-induced oxidation of Tyr residues was investigated using direct ionisation (via 266 nm light excitation) and sensitized photo-oxidation (by 3-carboxybenzophenone as sensitizer and 355 nm). Light emission (fluorescence) was observed at 410–440 nm as a result of Tyr oxidation. This novel light emission process is shown to be dependent on the solvent and aromatic ring substituents, however it does not depend on pH. It is proposed, that after initial formation of tyrosine phenoxyl radicals (TyrO●) by one electron-oxidation, the TyrO● absorbs a second photon to give an excited state species that undergoes subsequent light emission. The intensity of this emission depends on the Tyr concentration, and the detection of this emission can be used to identify and quantify one-electron formation of oxidized Tyr residues on proteins.

AB - Tyrosine residues (Tyr) on proteins are a favoured site of one-electron oxidation due to their low one-electron reduction potentials. In this work, light-induced oxidation of Tyr residues was investigated using direct ionisation (via 266 nm light excitation) and sensitized photo-oxidation (by 3-carboxybenzophenone as sensitizer and 355 nm). Light emission (fluorescence) was observed at 410–440 nm as a result of Tyr oxidation. This novel light emission process is shown to be dependent on the solvent and aromatic ring substituents, however it does not depend on pH. It is proposed, that after initial formation of tyrosine phenoxyl radicals (TyrO●) by one electron-oxidation, the TyrO● absorbs a second photon to give an excited state species that undergoes subsequent light emission. The intensity of this emission depends on the Tyr concentration, and the detection of this emission can be used to identify and quantify one-electron formation of oxidized Tyr residues on proteins.

UR - http://www.scopus.com/inward/record.url?scp=85083383472&partnerID=8YFLogxK

U2 - 10.1016/j.freeradbiomed.2020.03.022

DO - 10.1016/j.freeradbiomed.2020.03.022

M3 - Journal article

C2 - 32304751

AN - SCOPUS:85083383472

VL - 153

SP - 12

EP - 16

JO - Free Radical Biology & Medicine

JF - Free Radical Biology & Medicine

SN - 0891-5849

ER -

ID: 244531489