Proton hyperfine resonance assignments in cyanide-ligated cytochrome c peroxidase using the nuclear Overhauser effect.
The development of the proton nuclear Overhauser effect (NOE) for hyperfine shifted resonances of cyanide-ligated cytochrome c peroxidase (Saccharomyces cerevisiae) has been studied. In the pre-steady state regime, the major effects are due to primary NOEs to nearest neighbor protons. This has been used to advantage in making assignments of all of the remaining unassigned, resolved, downfield hyperfine shifted resonances. This work also determined the relative orientation of the heme pyrrole II substituents which is the cis configuration with the 4 alpha-vinyl proton pointing away from the 3CH3. In addition to heme protons, resonances of histidine 175, threonine 180, and histidine 52 have been assigned. These results indicate some structural rearrangement of the distal amino acids accompanying ligation.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003486:Cyanides; D003578:Cytochrome-c Peroxidase; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010544:Peroxidases; D011522:Protons; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D003486:Cyanides; D011522:Protons; D010544:Peroxidases; D003578:Cytochrome-c Peroxidase