Amino acid-fe(II)-chelator complexes exhibit strong antioxidant activity. T
aking advantage of the unique spectral characteristics of the complexes for
med when Ferrozine (Fz) is used as the chelator, we now show that the prima
ry blue complex (epsilon (max) at 632 nm) decomposes by two independent pat
hways: (i) a nonoxidative pathway involving dissociation of the amino add c
omponent and formation of a purple complex (epsilon (max) at 562 nm) and (i
i) an oxidative pathway leading to Fe(lll) and colorless products. Quantita
tive conversion of the blue to purple complex yields an isosbestic point (i
.p.) at 601 nm, whereas no i.p. is formed during quantitative oxidation of
the blue complex. However, under some experimental conditions, decompositio
n of the blue product occurs by both pathways, leading to occurrence of a c
lean i.p. at wavelengths varying from 601 to 574 nm. Results of simulation
experiments, confirmed by direct analysis, demonstrate that shifts in the i
.p. reflect differences in the fractions of blue compound that decompose by
the oxidative and nonoxidative pathways. Indeed, the fraction of blue that
is converted to the purple complex is readily deduced from the wavelength
of the i.p. These results suggest that identification of a physiological ch
elator that can replace Ferrozine in amino acid-iron complexes might have i
mportant physiological and pharmacological applications.