Superoxide-dependent formation of hydroxyl radicals from ferric-complexes and hydrogen peroxide: an evaluation of fourteen iron chelators.
When a variety of ferric chelates are reacted with hydrogen peroxide in phosphate buffer deoxyribose is damaged and this damage is protected against by formate, thiourea and mannitol. Damage done by ferric complexes of citrate, EDTA, NTA, EGTA and HEDA is substantially inhibited by superoxide dismutase (SOD) whereas complexes of PLA, ADP and CDTA are moderately inhibited by SOD. The effects of SOD argue against hydrogen peroxide acting as a reductant in Fenton chemistry driven by ferric complexes and hydrogen peroxide. EDTA has proved to be a useful model for Fenton chemistry that is inhibited by SOD although, it is not unique in this respect.
Gutteridge
J M
JM
Molecular Toxicology, Oklahoma Medical Research Foundation, Oklahoma City 73104.
D055598:Chemical Phenomena; D002621:Chemistry; D002951:Citrates; D019343:Citric Acid; D003855:Deoxyribose; D004492:Edetic Acid / Q000031:analogs & derivatives; D006861:Hydrogen Peroxide; D006878:Hydroxides; D017665:Hydroxyl Radical; D007502:Iron Chelating Agents / Q000494:pharmacology; D009571:Nitrilotriacetic Acid; D013481:Superoxides / Q000494:pharmacology*
D002951:Citrates; D006878:Hydroxides; D007502:Iron Chelating Agents; D013481:Superoxides; D019343:Citric Acid; D017665:Hydroxyl Radical; D003855:Deoxyribose; D004492:Edetic Acid; D006861:Hydrogen Peroxide; D009571:Nitrilotriacetic Acid; C026060:N-(hydroxyethyl)ethylenediaminetriacetic acid