The reductions of a number of sperm-whale Fe(III) myoglobin-ligand complexes by electrons generated by gamma-irradiation in ethylene glycol/water glass, have been investigated by using low-temperature spectrophotometry. The ligands are azide, fluoride, imidazole and water. 2. The reduction of the Fe(III) myoglobin-ligand complexes at 77 K leads to the formation of low-spin liganded Fe(II) myoglobin, in the case of the azide, imidazole and water derivatives, while the reduction of the fluoride derivative proceeds both by a pathway involving prior dissociation of the ligand and with the ligand in position. 3. Investigation of the effect of temperature on the stability of the Fe(II) myoglobin-ligand complexes indicates that more than one bound states exists in dissociation of the ligand molecule from the ferrous heme iron of the reduced azide and imidazole derivatives. 4. The results are discussed in terms of the possible structure of the Fe(II) myoglobin complexes and it is suggested that the low-spin state is created by a strained configuration of the heme center with the iron atom in an intermediate position relative to the heme plane.
