The fact that the siderophore ligand shows strong affinity for only the higher oxidation state of iron sets this natural com- plexing agent apart from molecules such as heme, which serve effectively as electron shuttles. At the same time, the relatively weak complexing of Fe(II) affords an efficient means of release, via reduction, inside the cell. This large discrepancy in the binding constants for Fe(II) and Fe(III) drives down the oxida- tion-reduction potential, and there has been some discussion that the actual value may be beyond the range of natural reducing agents. This aspect of the problem requires clarifica- tion and elucidation at the enzyme level. Probably the signifi- cant feature is the oxidation-reduction potential of the enzyme- ferric siderophore complex rather than the potential of the free ferric chelate.
With few exceptions, the “hard” acid ion, Fe(III), is linked to hard base atoms, such as oxygen, which accounts for the pref- erence for ferric ion. Chirality in the ligand means that the binding sites for the metal ion are disposed in space in a particular orientation, and, hence, optical isomers are possible (10). Thus, ferrichrome (Fig. 1)