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Mössbauer spectra of a polycrystalline form of oxidized chloro‐5,10,15,20‐tetra(mesityl)porphyrin‐ atoiron(III) [Fe(TMP)Cl], compound A, were recorded over a range of temperatures (4.2–195 K) and magnetic fields (0–6 T). These spectra of compound A exhibit magnetic features which are markedly different from those of the analogous protein complexes, horse radish peroxidase compound I (HRP‐I) and compound ES of cytochrome c peroxidase, even though chemical evidence and optical spectroscopy indicate that compound A is similar to the others in comprising a Fe(IV) complex within a porphyrin cation radical. We interpret the data by employing a spin Hamiltonian model in which the central Fe(IV) complex, with S=1, is tightly coupled to a S=1/2 system of the oxidized porphyrin to yield a net S=3/2 system as suggested by the susceptibility measurements. The theoretical treatment yields information on the d‐electron energies which is similar to that more directly available in the peroxidase spectra. The strength of the axial crystal field is found to increase progressively in the series HRP‐I, ES, compound A, while the spin coupling in A is the strongest of the three by several orders of magnitude. The good fits to experimental data confirm the efficacy of the theoretical treatment which may be applicable to a variety of other coupled systems

Mössbauer effect study of tight spin coupling in oxidized chloro-5,10,15,20-tetra(mesityl)porphyrinatoiron(III)