title: Proton NMR studies of horse ferricytochrome c. Completion of the assignment of the well resolved hyperfine shifted resonances.
abstract: 1H NMR saturation transfer and nuclear Overhauser effect (NOE) measurements have been used together with two-dimensional spectra to complete the assignment of the well resolved hyperfine shifted resonances in the spectrum of horse ferricytochrome c and obtain their shifts in the reduced protein. New assignments include the beta-CH2 protons of Met-80, both ring protons of His-18, and the alpha-CH2 of Gly-29 and delta-CH2 of Pro-30, which resonate surprisingly far upfield despite the absence of any Fermi contact contribution to the shift.
authors.affiliation: Centro de Quimica Estrutural, UNL, Lisboa, Portugal.
authors.forename: H
authors.initials: H
authors.lastname: Santos
authors.forename: D L
authors.initials: DL
authors.lastname: Turner
mesh_terms: D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D006418:Heme; D006736:Horses; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D003574:Cytochrome c Group; D006418:Heme