Multiple forms of sulfmyoglobin as detected by 1H nuclear magnetic resonance spectroscopy.
The proton nuclear magnetic resonance spectrum of sulfmyoglobin prepared in standard fashion reveals the presence of three forms, A, B, and C, with different chemical reactivity. Conditions for some interconversions of these forms are given. The 1H NMR spectra of the different forms show similar patterns. It appears that the differences between forms involve chemical modification on the porphyrin periphery. The altered heme can be extracted from FeIII(CN) sulfmyoglobin C to give a stable green substance.
D000818:Animals; D003486:Cyanides; D005290:Ferric Compounds; D006418:Heme / Q000031:analogs & derivatives; D009682:Magnetic Resonance Spectroscopy; D009211:Myoglobin / Q000031:analogs & derivatives*; D011166:Porphyrins; D011487:Protein Conformation; D014907:Whales
D003486:Cyanides; D005290:Ferric Compounds; D009211:Myoglobin; D011166:Porphyrins; C043848:sulfmyoglobin; D006418:Heme