Nuclear‐Magnetic‐Resonance Studies of Eukaryotic Cytochrome c

Abstract
The aromatic regions of the nuclear magnetic resonance spectra of horse ferricytochrome c and horse ferrocytochrome c are described. Resonance assignments have been made using NMR double‐resonance techniques, spectral comparison of related proteins, the perturbing effects of extrinsic probes, and from knowledge of the X‐ray structure of cytochrome c. 33 resonances arising from 39 aromatic protons of ferrocytochrome c, and 18 resonances arising from 27 aromatic protons of ferricytochrome c have been assigned.