Electron paramagnetic resonance studies of highly anisotropic low-spin states of ferrimyoglobin derivatives.
The effects of addition of nitrogenous bases, which gave low-spin ferric porphyrin complexes with highly anisotropic g values, were investigated for ferrimyoglobin by low-temperature EPR measurements. Concomitant denaturation of myoglobin upon addition of the exogenous bases was also of interest. By addition of pyridine-type bases under regulated pH, Mb(Fe3+) complexes showing EPR spectra with highly anisotropic g values were formed. These complexes have the electronic states close to the spin-crossover point but not so close as that of the ferric porphyrin highly anisotropic low-spin (HALS) complexes previously reported. Several types of low-spin species, LSi, LSa and LSb, were produced by the denaturation of myoglobin caused by addition of some exogenous ligands. The LSi was assigned to a complex with histidine-E7 coordinated on the sixth position and LSa to the one with OH- and histidine-F8[Im0].
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D006420:Hemeproteins; D006736:Horses; D007501:Iron / Q000032:analysis; D008024:Ligands; D008433:Mathematics; D008786:Metmyoglobin; D009132:Muscles; D011485:Protein Binding; D011487:Protein Conformation
D006420:Hemeproteins; D008024:Ligands; D008786:Metmyoglobin; D007501:Iron