EDTA inhibits peroxidase-catalyzed iodide oxidation through interaction at the iodide binding site.
EDTA inhibits the formation of I3- from iodide catalysed by various pure peroxidases. The inhibition is concentration-dependent and chloroperoxidase (CPO) is more sensitive than horseradish peroxidase (HRP) and lactoperoxidase (LPO). EDTA is more active than EGTA or other biological chelators tested. Zn2+, Mn2+ and Co2+ are equally active in reversing the effect of EDTA on both CPO and HRP almost completely, but ineffective in the case of LPO. The effect of EDTA on HRP can be reversed by a higher concentration of iodide but not by H2O2. EDTA causes a hypsochromic change in the absorption of the Soret band of HRP at 402 nm, and iodide can reverse this effect. EDTA can effectively displace radioiodide specifically bound to HRP. It is suggested that EDTA inhibits iodide oxidation by interacting at the iodide binding site of the HRP.
Banerjee
R K
RK
Department of Physiology, Indian Institute of Chemical Biology, Calcutta, India.
D002711:Chloride Peroxidase / Q000037:antagonists & inhibitors*; D004492:Edetic Acid / Q000494:pharmacology*; D006735:Horseradish Peroxidase / Q000037:antagonists & inhibitors*; D007454:Iodides / Q000378:metabolism*; D007700:Kinetics; D007784:Lactoperoxidase / Q000037:antagonists & inhibitors*; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000037:antagonists & inhibitors*
D007454:Iodides; D004492:Edetic Acid; D006735:Horseradish Peroxidase; D007784:Lactoperoxidase; D010544:Peroxidases; D002711:Chloride Peroxidase