Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c

The structure of oxidized and reduced forms of the iso-1-cytochrome c of Saccharomyces cerevisiae was analyzed by nuclear magnetic resonance spectroscopy. Iso-1-cytochrome exhibited high RMSD values in D2O solutions with large numbers of amide NH due to the the rigidity of the cytochrome backbone compared to the cyanide adduct of the Ala 80 protein. Furthermore, iso-1-cytochrome also exhibited hydrogen-bond networks and an additional helix in its 15-18 residues.