Effects of a thiolate axial ligand on the π→π* electronic states of oxoferryl porphyrins:: a study of the optical and resonance Raman spectra of compounds I and II of chloroperoxidase

Optical absorption and resonance Raman spectra have been investigated for enzymatic intermediates, compounds I and II, of chloroperoxidase (CPO) which contains a thiolate-ligated iron porphyrin. Compound I of CPO (CPO-I), an oxoferryl porphyrin pi cation radical, gave an apparently asymmetric single-peaked Soret band at 367 nm, for which band fitting analyses revealed the presence of two transition bands around 365 and 415 nm. Compound II of CPO (CPO-II), an oxoferryl neutral porphyrin, gave a split Soret spectrum with two bands (blue and red Soret bands) at 373 and 436 nm. Thus both CPO-I and CPO-II can be categorized as hyperporphyrins, The maximum extinction coefficients (epsilon (b) and epsilon (r)) and energies (E-b and E-r) of the blue and red Soret bands of CPO-II were found to fall on an epsilon (b)/epsilon (r) versus E-b-E-r correlation line derived from data reported for six-coordinate ferrous derivatives of cytochrome P450 and CPO, Corresponding data for CPO-I did not fall on the correlation line. Resonance enhancement of the Fe-IV=O stretching (nu (FeO)) Raman band was found for CPO-I when Raman scattering was excited at wavelengths within both transition bands around 365 and 415 nm, while the nu (FeO) Raman band was not identified for CPO-II at any of the excitation wavelengths examined here. These findings suggest that the thiolate axial ligand causes Soret band splitting of CPO-II through configuration interaction between the sulfurt-->porphyrin e(g)* charge transfer and porphyrin a(1u),a(2u)-->e(g)* transitions, while the FeO portion is important in determining the shape of the Soret band of CPO-I.