Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin.
The hyperfine shifted resonances arising from all four individual haem carbons of the paramagnetic low-spin met-cyano complex of sperm whale myoglobin have been clearly identified and assigned for the first time with the aid of 1H-13C heteronuclear chemical shift correlated spectroscopy. Alteration of the in-plane symmetry of the electronic structure of haem induced by the ligation of proximal histidyl imidazole spreads the haem carbon resonances to 32 ppm at 22 degrees C, indicating the sensitivity of those resonances to the haem electronic/molecular structure. Those resonances are potentially powerful probes in characterizing the nature of haem electronic structure.
D000818:Animals; D006418:Heme; D006420:Hemeproteins; D006639:Histidine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008786:Metmyoglobin / Q000031:analogs & derivatives; D011487:Protein Conformation; D014907:Whales
D006420:Hemeproteins; C007177:cyanometmyoglobin; D008786:Metmyoglobin; D006418:Heme; D006639:Histidine