1H NMR studies at 360 MHz of the aromatic amino acid residues in ferrocytochrome c-552 from Euglena gracilis.
The resonances of the aromatic rings in the 1H NMR spectra at 360 MHz of ferrocytochrome c-552 of Euglena gracilis were investigated by double resonance techniques. The spin systems of the two tryptophan and four of the tyrosine residues could be identified. This analysis of the aromatic region of the 1H NMR spectrum provided evidence that His-14 is bound to the heme iron. It gave also some insight into the molecular dynamics of ferrocytochrome c-552 in that it showed that of the six aromatic rings, four tyrosines were rotating rapidly about the Cbeta-Cgamma bond, while one tyrosine and the single phenylalanine were restricted in their rotational mobilities by their environmnent in the protein.
D000818:Animals; D001665:Binding Sites; D003574:Cytochrome c Group; D005056:Euglena gracilis / Q000201:enzymology*; D006418:Heme; D007501:Iron; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011487:Protein Conformation; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000032:analysis
D003574:Cytochrome c Group; D014443:Tyrosine; D006418:Heme; D014364:Tryptophan; D007501:Iron