Structural role of the tyrosine residues of cytochrome c.
The tertiary structures of horse, tuna, Neurospora crassa, horse [Hse65,Leu67]- and horse [Hse65,Leu74]-cytochromes c were studied with high-resolution 1H n.m.r. spectroscopy. The amino acid sequences of these proteins differ at position 46, which is occupied by phenylalanine in the horse proteins but by tyrosine in the remaining two, and at positions 67, 74 and 97, which are all occupied by tyrosine residues in horse and tuna cytochrome c but in the other proteins are substituted by phenylalanine or leucine, though there is only one such substitution per protein. The various aromatic-amino-acid substitutions do not seriously affect the protein structure.
D000595:Amino Acid Sequence; D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D006714:Homoserine / Q000032:analysis; D006736:Horses; D007930:Leucine / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D009492:Neurospora crassa; D010649:Phenylalanine / Q000032:analysis; D011487:Protein Conformation; D013696:Temperature; D014413:Tuna; D014443:Tyrosine / Q000032:analysis*
D003574:Cytochrome c Group; D014443:Tyrosine; D010649:Phenylalanine; D006714:Homoserine; D007930:Leucine