Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c

Cyanide-ligated cytochrome C peroxidase (CcP(N), horse ferricyte C and yeast isozyme-1 ferricyt C) reveals proton NMR spectra that show prominent modifications due to the stimulation by production a complex. Complexes with resting-state Ccp and ferricytochromes C show similar alterations. The heme active site of CcPCN is the destination of the transmission of ferricyte C binding. The solution-state conformation of the complexes resembles the pattern of shifts stimulated by heme pyrrole C replacements and the heme pyrrole. A replacements yield important CcPCN NMR shifts that are stimulated by complexes.