title: 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
abstract: 1H nuclear Overhauser effect experiments on the isotropically shifted signals of oxidized Chromatium vinosum HiPIP have been used to identify the four beta-CH2 geminal couples of the cysteine ligands. A partial assignment to individual residues has been proposed from a computer graphics analysis of the X-ray structure. Tentative assignments of other resonances are discussed.
authors.affiliation: Evans Laboratory of Chemistry, Ohio State University, Columbus 43210.
authors.forename: J A
authors.initials: JA
authors.lastname: Cowan
authors.forename: M
authors.initials: M
authors.lastname: Sola
mesh_terms: D001426:Bacterial Proteins; D002844:Chromatium; D003545:Cysteine; D007506:Iron-Sulfur Proteins; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins; D015394:Molecular Structure; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D045322:Photosynthetic Reaction Center Complex Proteins; C007943:high potential iron-sulfur protein; D003545:Cysteine