Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides

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Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides. / Winterbourn, Christine C; Parsons-Mair, Helena N; Gebicki, Silvia; Gebicki, Janusz M; Davies, Michael Jonathan.

In: Biochemical Journal, Vol. 381, No. Pt 1, 01.07.2004, p. 241-8.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Winterbourn, CC, Parsons-Mair, HN, Gebicki, S, Gebicki, JM & Davies, MJ 2004, 'Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides', Biochemical Journal, vol. 381, no. Pt 1, pp. 241-8. https://doi.org/10.1042/BJ20040259

APA

Winterbourn, C. C., Parsons-Mair, H. N., Gebicki, S., Gebicki, J. M., & Davies, M. J. (2004). Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides. Biochemical Journal, 381(Pt 1), 241-8. https://doi.org/10.1042/BJ20040259

Vancouver

Winterbourn CC, Parsons-Mair HN, Gebicki S, Gebicki JM, Davies MJ. Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides. Biochemical Journal. 2004 Jul 1;381(Pt 1):241-8. https://doi.org/10.1042/BJ20040259

Author

Winterbourn, Christine C ; Parsons-Mair, Helena N ; Gebicki, Silvia ; Gebicki, Janusz M ; Davies, Michael Jonathan. / Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides. In: Biochemical Journal. 2004 ; Vol. 381, No. Pt 1. pp. 241-8.

Bibtex

@article{81547cd0e55d4c9887db34f650148b97,
title = "Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides",
abstract = "Superoxide reacts rapidly with other radicals, but these reactions have received little attention in the context of oxidative stress. For tyrosyl radicals, reaction with superoxide is 3-fold faster than dimerization, and forms the addition product tyrosine hydroperoxide. We have explored structural requirements for hydroperoxide formation using tyrosine analogues and di- and tri-peptides. Superoxide and phenoxyl radicals were generated using xanthine oxidase, peroxidase and the respective tyrosine derivative, or by gamma-radiation. Peroxides were measured using FeSO4/Xylenol Orange. Tyrosine and tyramine formed stable hydroperoxides, but N-acetyltyrosine and p-hydroxyphenylacetic acid did not, demonstrating a requirement for a free amino group. Using [14C]tyrosine, the hydroperoxide and dityrosine were formed at a molar ratio of 1.8:1. Studies with pre-formed hydroperoxides, and measurements of substrate losses, indicated that, in the absence of a free amino group, reaction with superoxide resulted primarily in restitution of the parent compound. With dipeptides, hydroperoxides were formed only on N-terminal tyrosines. However, adjacent lysines promoted hydroperoxide formation, as did addition of free lysine or ethanolamine. Results are compatible with a mechanism [d'Alessandro, Bianchi, Fang, Jin, Schuchmann and von Sonntag (2000) J. Chem. Soc. Perkin Trans. II, 1862-1867] in which the phenoxyl radicals react initially with superoxide by addition, and the intermediate formed either releases oxygen to regenerate the parent compound or is converted into a hydroperoxide. Amino groups favour hydroperoxide formation through Michael addition to the tyrosyl ring. These studies indicate that tyrosyl hydroperoxides should be formed in proteins where there is a basic molecular environment. The contribution of these radical reactions to oxidative stress warrants further investigation.",
keywords = "Amines, Dimerization, Free Radicals, Hydrogen Peroxide, Models, Chemical, Peptides, Superoxides, Tyrosine",
author = "Winterbourn, {Christine C} and Parsons-Mair, {Helena N} and Silvia Gebicki and Gebicki, {Janusz M} and Davies, {Michael Jonathan}",
year = "2004",
month = "7",
day = "1",
doi = "10.1042/BJ20040259",
language = "English",
volume = "381",
pages = "241--8",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "Pt 1",

}

RIS

TY - JOUR

T1 - Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides

AU - Winterbourn, Christine C

AU - Parsons-Mair, Helena N

AU - Gebicki, Silvia

AU - Gebicki, Janusz M

AU - Davies, Michael Jonathan

PY - 2004/7/1

Y1 - 2004/7/1

N2 - Superoxide reacts rapidly with other radicals, but these reactions have received little attention in the context of oxidative stress. For tyrosyl radicals, reaction with superoxide is 3-fold faster than dimerization, and forms the addition product tyrosine hydroperoxide. We have explored structural requirements for hydroperoxide formation using tyrosine analogues and di- and tri-peptides. Superoxide and phenoxyl radicals were generated using xanthine oxidase, peroxidase and the respective tyrosine derivative, or by gamma-radiation. Peroxides were measured using FeSO4/Xylenol Orange. Tyrosine and tyramine formed stable hydroperoxides, but N-acetyltyrosine and p-hydroxyphenylacetic acid did not, demonstrating a requirement for a free amino group. Using [14C]tyrosine, the hydroperoxide and dityrosine were formed at a molar ratio of 1.8:1. Studies with pre-formed hydroperoxides, and measurements of substrate losses, indicated that, in the absence of a free amino group, reaction with superoxide resulted primarily in restitution of the parent compound. With dipeptides, hydroperoxides were formed only on N-terminal tyrosines. However, adjacent lysines promoted hydroperoxide formation, as did addition of free lysine or ethanolamine. Results are compatible with a mechanism [d'Alessandro, Bianchi, Fang, Jin, Schuchmann and von Sonntag (2000) J. Chem. Soc. Perkin Trans. II, 1862-1867] in which the phenoxyl radicals react initially with superoxide by addition, and the intermediate formed either releases oxygen to regenerate the parent compound or is converted into a hydroperoxide. Amino groups favour hydroperoxide formation through Michael addition to the tyrosyl ring. These studies indicate that tyrosyl hydroperoxides should be formed in proteins where there is a basic molecular environment. The contribution of these radical reactions to oxidative stress warrants further investigation.

AB - Superoxide reacts rapidly with other radicals, but these reactions have received little attention in the context of oxidative stress. For tyrosyl radicals, reaction with superoxide is 3-fold faster than dimerization, and forms the addition product tyrosine hydroperoxide. We have explored structural requirements for hydroperoxide formation using tyrosine analogues and di- and tri-peptides. Superoxide and phenoxyl radicals were generated using xanthine oxidase, peroxidase and the respective tyrosine derivative, or by gamma-radiation. Peroxides were measured using FeSO4/Xylenol Orange. Tyrosine and tyramine formed stable hydroperoxides, but N-acetyltyrosine and p-hydroxyphenylacetic acid did not, demonstrating a requirement for a free amino group. Using [14C]tyrosine, the hydroperoxide and dityrosine were formed at a molar ratio of 1.8:1. Studies with pre-formed hydroperoxides, and measurements of substrate losses, indicated that, in the absence of a free amino group, reaction with superoxide resulted primarily in restitution of the parent compound. With dipeptides, hydroperoxides were formed only on N-terminal tyrosines. However, adjacent lysines promoted hydroperoxide formation, as did addition of free lysine or ethanolamine. Results are compatible with a mechanism [d'Alessandro, Bianchi, Fang, Jin, Schuchmann and von Sonntag (2000) J. Chem. Soc. Perkin Trans. II, 1862-1867] in which the phenoxyl radicals react initially with superoxide by addition, and the intermediate formed either releases oxygen to regenerate the parent compound or is converted into a hydroperoxide. Amino groups favour hydroperoxide formation through Michael addition to the tyrosyl ring. These studies indicate that tyrosyl hydroperoxides should be formed in proteins where there is a basic molecular environment. The contribution of these radical reactions to oxidative stress warrants further investigation.

KW - Amines

KW - Dimerization

KW - Free Radicals

KW - Hydrogen Peroxide

KW - Models, Chemical

KW - Peptides

KW - Superoxides

KW - Tyrosine

U2 - 10.1042/BJ20040259

DO - 10.1042/BJ20040259

M3 - Journal article

VL - 381

SP - 241

EP - 248

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - Pt 1

ER -

ID: 138274116