Nuclear magnetic resonance studies of hemoproteins. VIII. Proton NMR studies of the binding of various nitrogenous ligands to ferric cytochrome c.
The structure of the heme environment of horse heart ferric cytochrome c was examined in the presence of various nitrogenous bases at several temperatures with the aid of hyperfine shifted proton NMR spectra at 220 MHz. The resonance positions and line widths of the signals for the peripheral methyl groups of the heme exhibited distinctive features of its low-spin state characteristic of each external ligand. In the imidazole complex of ferric cytochrome c, remarkable line sharpening of the heme-linked proton signals was encountered on raising the temperature. This may be related to the apoprotein perturbation on the binding of external ligand to the heme iron. These spectral peculiarities were discussed in relation to the electronic structure of the heme, the basicity of the external ligand and the van der Waals contact interaction between heme side chains and apoprotein.
D000588:Amines; D000818:Animals; D003574:Cytochrome c Group; D006736:Horses; D007093:Imidazoles; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D009206:Myocardium / Q000201:enzymology; D011487:Protein Conformation; D011725:Pyridines
D000588:Amines; D003574:Cytochrome c Group; D007093:Imidazoles; D008024:Ligands; D011725:Pyridines