DIRECT RESONANCE RAMAN EVIDENCE FOR A TRANS INFLUENCE ON THE FERRYL FRAGMENT IN MODELS OF COMPOUND-I INTERMEDIATES OF HEME ENZYMES

Resonance Raman (RR) spectra are reported for a series of ferric compl exes of meso-tetramesitylporphyrin XFe(III)(TMP) (where X = F-, Cl-, m -chlorobenzoate (mCB(-)), CF3O2SO- (trif(-)) and ClO4-) and their oxid ized derivatives, OFeIV(TMP(.+))(X). Mode assignments are made by RR s tudies of the beta-pyrrole-deuterated and O-18-labeled analogues. The results demonstrate that the oxo-iron bond strength is sensitive to th e nature of the transaxial ligand (X), the nu(Fe=O) stretching mode ap pearing near 800 cm(-1) for the F-, Cl-, and mCB(-) complexes and near 835 cm(-1) for the trif(-) and ClO4- complexes. The high-frequency ma rker modes and the H-1 chemical shifts are consistent with stronger el ectron donation by the former three anions. An explanation for the app arent absence of a correlation between the nu(Fe=O) stretching frequen cies and the previously reported rate constants for substrate epoxidat ion is also suggested.