The addition of chelated Fe 2 + ions in a liposomal system often results in a short lag period before peroxidation starts. The addition of a second chelator at the end of the lag period results in an inhibition of the lipid peroxidation. The degree of inhibition depends on the stability constants of the chelator in ligating Fe 2 + and/or Fe 3 + . A more striking inhibitory effect was observed for the chelators with higher stability constant for either or both Fe 2 + - and Fe 3 + -complex, but much less inhibition was found for those with lower stability constants for both complexes. Assuming that the initiator for iron-dependent lipid peroxidation is formed through the redox process of iron ion and finally emerged at the end of the latent period, the inhibitory effect of the second chelator may be explained as the abstraction of either Fe 2 + or Fe 3 + from the initiator by an additional free chelator, which results in the decomposition of the initiator. This study supports the hypothesis that a Fe 2 + Fe 3 + complex is responsible for iron-initiated lipid peroxidation.