1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the hyperfine-shifted signals of deoxymyoglobin. The nuclear longitudinal-relaxation-time values indicate short electron-relaxation times whereas Curie relaxation contributes significantly to the signals linewidths. For reduced cytochrome P450 the linewidths are larger due to the Curie-relaxation contribution in a large protein. Therefore, the spectral information is poor. The electron-relaxation rates are discussed in terms of possible electronic structure.
Banci
L
L
Department of Chemistry, University of Florence, Italy.
Bertini
I
I
Marconi
S
S
Pierattelli
R
R
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D009211:Myoglobin / Q000031:analogs & derivatives* / Q000737:chemistry; D010084:Oxidation-Reduction; D016958:Pseudomonas putida / Q000737:chemistry; D014907:Whales
D009211:Myoglobin; C055547:deoxymyoglobin; D003577:Cytochrome P-450 Enzyme System