Proton nmr spectroscopy of high-spin ferrous cytochrome P-450 models.
Alkyl mercaptide complexes of both synthetic and natural-derivative iron(II) porphyrins have been characterized in DMSO solution by proton nmr spectroscopy. A single mercaptide ligand binds to form a high-spin iron(II) complex as determined by solution magnetic measurements and the nmr isotropic shift pattern. Ligand exchange is slow on the nmr time scale unlike corresponding 2-methyl-imidazole exchange rates which are very rapid. Further comparison of mercaptide and 2-methyl imidazole adducts reveals a downfield bias in isotropic shift values for the mercaptide species, which may be explained by different signs in the dipolar shift term for the two complexes. This apparent magnetic anisotropy of the mercaptide complex is in the same direction, although smaller, than that observed for bacterial cytochrome P-450. Isotropic shift values of at least 250 ppm for methylene resonances of the coordinated mercaptide support a very efficient unpaired spin delocalization for this axial ligand.
D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D011166:Porphyrins; D011485:Protein Binding
D008024:Ligands; D011166:Porphyrins; D003577:Cytochrome P-450 Enzyme System; D007501:Iron