Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants

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Myoglobin-induced oxidative damage : evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. / Irwin, J A; Ostdal, H; Davies, Michael Jonathan.

In: Archives of Biochemistry and Biophysics, Vol. 362, No. 1, 01.02.1999, p. 94-104.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Irwin, JA, Ostdal, H & Davies, MJ 1999, 'Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants', Archives of Biochemistry and Biophysics, vol. 362, no. 1, pp. 94-104. https://doi.org/10.1006/abbi.1998.0987

APA

Irwin, J. A., Ostdal, H., & Davies, M. J. (1999). Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Archives of Biochemistry and Biophysics, 362(1), 94-104. https://doi.org/10.1006/abbi.1998.0987

Vancouver

Irwin JA, Ostdal H, Davies MJ. Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Archives of Biochemistry and Biophysics. 1999 Feb 1;362(1):94-104. https://doi.org/10.1006/abbi.1998.0987

Author

Irwin, J A ; Ostdal, H ; Davies, Michael Jonathan. / Myoglobin-induced oxidative damage : evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. In: Archives of Biochemistry and Biophysics. 1999 ; Vol. 362, No. 1. pp. 94-104.

Bibtex

@article{04405bb7474841619038e39db0db72af,
title = "Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants",
abstract = "Reaction of equine Fe(III) myoglobin with H2O2 gives rise to an Fe(IV)-oxo species at the heme center and protein (globin)-derived radicals. Studies have shown that there are two (or more) sites for the protein-derived radical: at tyrosine (Tyr-103) or tryptophan (Trp-14). The latter radical reacts rapidly with oxygen to give a Trp-derived peroxyl radical. The formation of both the tyrosine phenoxyl radical and the tryptophan-derived peroxyl species have been confirmed in the present study; the latter appears to be the major initial radical, with the phenoxyl radical appearing at longer reaction times, possibly via secondary reactions. We have investigated, by EPR spectroscopy, the reactivity of the Trp-14 peroxyl radical with amino acids, peptides, proteins, and antioxidants, with the aim of determining whether this species can damage other targets, i.e., whether intermolecular protein-to-protein radical transfer and hence chain-oxidation occurs, and the factors that control these reactions. Three amino acids show significant reactivity: Tyr, Trp, and Cys, with Cys the least efficient. Evidence has also been obtained for (inefficient) hydrogen abstraction at peptide alpha-carbon sites; this may result in backbone cleavage in the presence of oxygen. The myoglobin Trp-14 peroxyl radical has been shown to react rapidly with a wide range of proteins to give long-lived secondary radicals on the target protein. These reactions appear to mainly involve Tyr residues on the target protein, although evidence for reaction at Trp has also been obtained. Antioxidants (GSH, ascorbate, Trolox C, vitamin E, and urate) react with the myoglobin-derived peroxyl radical; in some cases antioxidant-derived radicals are detected. These reactions are only efficient at high antioxidant concentrations, suggesting that protein-to-protein damage transfer and protein chain-oxidation may occur readily in biological systems.",
keywords = "Amino Acids, Animals, Antioxidants, Cattle, Free Radicals, Horses, Metmyoglobin, Myoglobin, Oxidation-Reduction, Oxidative Stress, Peptides, Proteins",
author = "Irwin, {J A} and H Ostdal and Davies, {Michael Jonathan}",
note = "Copyright 1999 Academic Press.",
year = "1999",
month = "2",
day = "1",
doi = "10.1006/abbi.1998.0987",
language = "English",
volume = "362",
pages = "94--104",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - Myoglobin-induced oxidative damage

T2 - evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants

AU - Irwin, J A

AU - Ostdal, H

AU - Davies, Michael Jonathan

N1 - Copyright 1999 Academic Press.

PY - 1999/2/1

Y1 - 1999/2/1

N2 - Reaction of equine Fe(III) myoglobin with H2O2 gives rise to an Fe(IV)-oxo species at the heme center and protein (globin)-derived radicals. Studies have shown that there are two (or more) sites for the protein-derived radical: at tyrosine (Tyr-103) or tryptophan (Trp-14). The latter radical reacts rapidly with oxygen to give a Trp-derived peroxyl radical. The formation of both the tyrosine phenoxyl radical and the tryptophan-derived peroxyl species have been confirmed in the present study; the latter appears to be the major initial radical, with the phenoxyl radical appearing at longer reaction times, possibly via secondary reactions. We have investigated, by EPR spectroscopy, the reactivity of the Trp-14 peroxyl radical with amino acids, peptides, proteins, and antioxidants, with the aim of determining whether this species can damage other targets, i.e., whether intermolecular protein-to-protein radical transfer and hence chain-oxidation occurs, and the factors that control these reactions. Three amino acids show significant reactivity: Tyr, Trp, and Cys, with Cys the least efficient. Evidence has also been obtained for (inefficient) hydrogen abstraction at peptide alpha-carbon sites; this may result in backbone cleavage in the presence of oxygen. The myoglobin Trp-14 peroxyl radical has been shown to react rapidly with a wide range of proteins to give long-lived secondary radicals on the target protein. These reactions appear to mainly involve Tyr residues on the target protein, although evidence for reaction at Trp has also been obtained. Antioxidants (GSH, ascorbate, Trolox C, vitamin E, and urate) react with the myoglobin-derived peroxyl radical; in some cases antioxidant-derived radicals are detected. These reactions are only efficient at high antioxidant concentrations, suggesting that protein-to-protein damage transfer and protein chain-oxidation may occur readily in biological systems.

AB - Reaction of equine Fe(III) myoglobin with H2O2 gives rise to an Fe(IV)-oxo species at the heme center and protein (globin)-derived radicals. Studies have shown that there are two (or more) sites for the protein-derived radical: at tyrosine (Tyr-103) or tryptophan (Trp-14). The latter radical reacts rapidly with oxygen to give a Trp-derived peroxyl radical. The formation of both the tyrosine phenoxyl radical and the tryptophan-derived peroxyl species have been confirmed in the present study; the latter appears to be the major initial radical, with the phenoxyl radical appearing at longer reaction times, possibly via secondary reactions. We have investigated, by EPR spectroscopy, the reactivity of the Trp-14 peroxyl radical with amino acids, peptides, proteins, and antioxidants, with the aim of determining whether this species can damage other targets, i.e., whether intermolecular protein-to-protein radical transfer and hence chain-oxidation occurs, and the factors that control these reactions. Three amino acids show significant reactivity: Tyr, Trp, and Cys, with Cys the least efficient. Evidence has also been obtained for (inefficient) hydrogen abstraction at peptide alpha-carbon sites; this may result in backbone cleavage in the presence of oxygen. The myoglobin Trp-14 peroxyl radical has been shown to react rapidly with a wide range of proteins to give long-lived secondary radicals on the target protein. These reactions appear to mainly involve Tyr residues on the target protein, although evidence for reaction at Trp has also been obtained. Antioxidants (GSH, ascorbate, Trolox C, vitamin E, and urate) react with the myoglobin-derived peroxyl radical; in some cases antioxidant-derived radicals are detected. These reactions are only efficient at high antioxidant concentrations, suggesting that protein-to-protein damage transfer and protein chain-oxidation may occur readily in biological systems.

KW - Amino Acids

KW - Animals

KW - Antioxidants

KW - Cattle

KW - Free Radicals

KW - Horses

KW - Metmyoglobin

KW - Myoglobin

KW - Oxidation-Reduction

KW - Oxidative Stress

KW - Peptides

KW - Proteins

U2 - 10.1006/abbi.1998.0987

DO - 10.1006/abbi.1998.0987

M3 - Journal article

C2 - 9917333

VL - 362

SP - 94

EP - 104

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -

ID: 138283140