title: 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Florence, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Banci
authors.forename: I
authors.initials: I
authors.lastname: Bertini
authors.forename: S
authors.initials: S
authors.lastname: Marconi
authors.forename: R
authors.initials: R
authors.lastname: Pierattelli
mesh_terms: 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
chemical_list: D009211:Myoglobin; C055547:deoxymyoglobin; D003577:Cytochrome P-450 Enzyme System