Comparative EPR study on high-spin ferric porphine complexes and cytochrome P-450 having rhombic character.
Comparative EPR studies were made on two high-spin Fe(III) porphine model systems and mammalian liver microsomal cytochromes P-450, all of which exhibit approximately the same degrees of rhombicity in their EPR spectra. Comparison of g values and linewidths as a function of temperature, and of the microwave power saturation demonstrated that EPR characteristics of P-450 are more similar to the Fe(III) porphines having the thiolate axial ligand than in the other model systems, the mixed crystals of Fe(III) porphine with the corresponding free base porphine, in which no thiolate ligand is involved. There is, however, a discrepancy between P-450 and the model thiolates with respect to the size of the zero-field parameter D. These observations indicate that P-450 heme has essential structural features in common with thiolates but the Fe-S bond of P-450 may be modified from its normal orientation in model thiolates, probably as a result of the constraints imposed by the protein structure.
D000818:Animals; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System; D004578:Electron Spin Resonance Spectroscopy; D005290:Ferric Compounds; D006168:Guinea Pigs; D007501:Iron; D007700:Kinetics; D008433:Mathematics; D008665:Metalloporphyrins; D051379:Mice; D008810:Mice, Inbred C57BL; D008862:Microsomes, Liver / Q000201:enzymology; D008954:Models, Biological; D008968:Molecular Conformation; D011487:Protein Conformation; D011817:Rabbits; D051381:Rats; D013696:Temperature
D005290:Ferric Compounds; D008665:Metalloporphyrins; C015213:ferric porphine complex; D003577:Cytochrome P-450 Enzyme System; D007501:Iron