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The modulation of ferryl myoglobin formation and its oxidative effects on low density lipoproteins by nitric oxide
Author(s) -
Dee Gareth,
Rice-Evans Catherine,
Obeyesekera Sharmin,
Meraji Shokoufeh,
Jacobs Michael,
Bruckdorfer K.Richard
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81338-9
Subject(s) - myoglobin , nitric oxide , chemistry , oxidative phosphorylation , hemeprotein , heme , modulation (music) , photochemistry , biophysics , biochemistry , organic chemistry , enzyme , biology , physics , acoustics
This study has investigated the interactions between nitric oxide and haem protein radicals. The results demonstrate that nitric oxide interacts with activated ferrylmyoglobin species with reduction to metmyoglobin, but the extent and duration of the reduction depends on the relative concentrations of nitric oxide and hydrogen peroxide. Ferryl myoglobin has a much greater relative potential for oxidising polyunsaturated fatty acid side chains in low density lipoproteins than in cell membranes. The peroxidative response can be modulated by nitric oxide: ferryl myoglobin‐mediated peroxidation of LDL may be enhanced or suppressed by nitric oxide depending on the relative concentrations of NO and hydrogen peroxide.