Initiation of lipid peroxidation in liposomes by cysteine, glutathione, or dithiothreitol required iron, and was not inhibited by superoxide dismutase. The absence of superoxide involvement in thiol autoxidation was confirmed by the inability of superoxide dismutase to inhibit thiol reduction of cytochrome c. Furthermore, the rate of cytochrome c reduction by thiols was not decreased under anaerobic conditions. We suggest that lipid peroxidation initiated by thiols and iron occurs via direct reduction of iron. Control of cellular thiol autoxidation, and reactions occurring as a consequence, such as lipid peroxidation, must therefore involve chelation of transition metals to control their redox reactions.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Jul 16 1982|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology