1H NMR Studies of Eukaryotic Cytochrome c

Abstract
1H NMR resonance assignments in the spectra of horse, tuna, Neurmpora crassa and Candida krusei cyto‐chromes c are described. Assignments have been made using NMR double‐resonance techniques in conjunction with electron‐exchange experiments, spectral comparison of related proteins, and consideration of the X‐ray structure of tuna cytochrome c. Resonances arising from 11 residues of horse cytochrome c have been assigned.