ESR studies of A(1u) and A(2u) oxoiron(IV) porphyrin pi-cation radical complexes. Spin coupling between ferryl iron and A(1u)/A(2u) orbitals

This study shows the ESR spectra of oxoiron(IV) porphyrin pi-cation radicals of 1-8 in dichloromethane-methanol (5:1) mixture. We reported in a previous paper that oxoiron(IV) porphyrin pi-cation radicals of 1-4 are in an a(1u) radical state while those of 5-8 are in an a(2u) radical. The ESR spectra (g(perpendicular to)(eff) similar to 3.1 and g(parallel to)(eff) similar to 2.0) for the a(1u) radical complexes, 1-4, appear quite different from those reported previously for the oxoiron(IV) porphyrin pi-cation radical of 5 (g(y) = 4.5, g(x) = 3.6, and g(z) = 1.99). The unique ESR spectra of the a(1u) radical complexes rather resemble those of compound I from Micrococcus lysodeikticus catalase (CAT) and ascorbate peroxidase (ASP). This is the first examples to mimic the ESR spectra of compound I in the enzymes. From spectral analysis based on a spin Hamiltonian containing an exchange interaction, the ESR spectra of 1-4 can be explained as a moderate ferromagnetic state (J/D similar to 0.3) between ferryl S = 1 and the porphyrin pi-cation radical S' = 1/2. The magnitudes of zero-field splitting (D) for ferryl iron and isotropic J value, estimated from the temperature-dependence of the half-saturation power of the ESR signals, are similar to 28 and similar to+8 cm(-1)) respectively. A change in the electronegativity of the beta-pyrrole substituent hardly changes the ESR spectral feature while that of the meso-substituent slightly does owing to the change in the E/D value. On the basis of the present ESR results, we propose the a(1u) radical state for compound I of CAT and ASP.