Abstract:
:Reaction of metmyoglobin with peroxides is known to involve the formation, possibly via a porphyrin radical-cation, of a ferryl (iron(IV)-oxo) species and a protein radical; there is a little information available as to which of these species initiates the damage which is observed on incubating membrane fractions with such mixtures. It is shown in this study that the initial protein radical, which is a tyrosine phenoxyl radical centered at position 103 in the protein, does not react rapidly with erythrocyte membranes. However a tyrosine peroxyl radical, formed by addition of oxygen to this species, does react rapidly, and it is concluded that this radical, together with the ferryl species, is an important initiating species in myoglobin-induced lipid peroxidation.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Newman ES,Rice-Evans CA,Davies MJdoi
10.1016/0006-291x(91)91730-zsubject
Has Abstractpub_date
1991-09-30 00:00:00pages
1414-9issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(91)91730-Zjournal_volume
179pub_type
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