Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide

Ali, Feda E., Barnham, Kevin J., Barrow, Colin J. and Separovic, Frances 2004, Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide, Journal of inorganic biochemistry, vol. 98, no. 1, pp. 173-184.

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Title Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide
Author(s) Ali, Feda E.
Barnham, Kevin J.
Barrow, Colin J.
Separovic, Frances
Journal name Journal of inorganic biochemistry
Volume number 98
Issue number 1
Start page 173
End page 184
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2004-01
ISSN 0162-0134
1873-3344
Summary Metal-catalysed oxidation (MCO) reactions result in the formation of reactive oxygen species (ROS) in biological systems. These ROS cause oxidative stress that contributes to a number of pathological processes leading to a variety of diseases. Tyrosine is one residue that is very susceptible to oxidative modification and the formation of dityrosine (DT) and 3,4-dihydroxyphenylalanine (DOPA) have been widely reported in a number of diseases. However, the mechanisms of MCO of tyrosine in biological systems are poorly understood and require further investigation. In this study we investigated the mechanism of DT and DOPA formation by MCO using N-acetyl tyrosine ethyl ester as a model for tyrosine in proteins and peptides. The results showed that DT formation could be observed upon Cu2+/H2O2 oxidation at pH 7.4. Our results indicate that it is unlikely to be via Fenton chemistry since Cu+/H2O2 oxidative conditions did not lead to the formation of DT.
Language eng
Field of Research 060105 Cell Neurochemistry
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2004, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30023800

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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