Mössbauer spectra of a polycrystalline form of oxidized chloro-5,10,15,20-tetra(mesityl)porphyrinatoiron(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.
All Science Journal Classification (ASJC) codes
- General Physics and Astronomy
- Physical and Theoretical Chemistry