The low-spin end-on ferric peroxo heme intermediate has been proposed as an alternative reactive intermediate involved in the catalytic cycles of enzymes Such as nitric oxide synthase and cytochrome P450. This transient heme intermediate has never been captured using synthetic heme models. We demonstrate herein Our Success in the Solution preparation of Such an end-on ferric peroxo intermediate derived from a heme model, which features both a group hanging Over the porphyrin macrocycle and a covalently appended axial imidazole ligand, through one-electron reduction of its ferric superoxo precursor. The obtained ferric peroxo intermediate was further transformed into the corresponding ferric hydroperoxo species upon protonation. This heme model compound provides a convenient system for sequential preparation of the important and biologically relevant superoxo/peroxo/hydroperoxo heme intermediates through an oxygenation/one-electron reduction/protonation process similar to the mechanisms used by enzyme systems.