Kinetics of the chemiluminescence associated to the reaction between peroxyl radicals and proteins

Protein oxidation, mediated by peroxyl radicals derived from 2,2'-azobis(2-amidinopropane) dihydrochloride is sided by a significant visible chemiluminescence (CL). The light emission shows a complex dependence with the protein concentration and with the incubation time that cannot be interpret...

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Bibliographic Details
Published in:Journal of Protein Chemistry 2001-08, Vol.20 (6), p.479-485
Main Authors: Aspée, A, Lissi, E A
Format: Article
Language:English
Subjects:
Amino acids
Chemiluminescence
Chromans - chemistry
Excitation
Free radicals
Insulin - chemistry
Intermediates
Kinetics
Light emission
Luminescent Measurements
Oxidation
Oxidation-Reduction
Peroxides - chemistry
Peroxyl radicals
Proteins
Proteins - chemistry
Radicals
Recombination
Ribonuclease, Pancreatic - chemistry
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Summary:Protein oxidation, mediated by peroxyl radicals derived from 2,2'-azobis(2-amidinopropane) dihydrochloride is sided by a significant visible chemiluminescence (CL). The light emission shows a complex dependence with the protein concentration and with the incubation time that cannot be interpreted in terms of peroxyl radicals recombination (Russell's mechanism). In all the systems studied, the chemiluminescent behavior requires to consider the participation of several oxidation products as precursors of the excited states. These compounds lead to the formation of excited states by competing radical and nonradical mediated pathways. These intermediates (most probably hydroperoxide-like compounds) would arise from the oxidation of Trp and Tyr residues. This conclusion is based on the similarity of the time profile of the chemiluminescence observed in the oxidation of the free amino acids and the proteins, both in the presence of and absence of free-radical scavengers.
ISSN:0277-8033
1572-3887
1573-4943
DOI:10.1023/A:1012554429450