15N resonance assignments of oxidized and reduced Chromatium vinosum high-potential iron protein.
The 15N resonances in reduced and oxidized Chromatium vinosum high-potential iron protein have been assigned by use of 1H-1H COSY spectra and 1H-15N HMQC. HMQC-COSY, and HMQC-NOESY spectra. Unambiguous assignment of 70 of 85 backbone 15N resonances in the reduced protein and 62 of 85 resonances in the oxidized protein are made, as are 12 of 21 side-chain 15N resonances.
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Evans Laboratory of Chemistry, Ohio State University, Columbus 43210, USA.
Cottrell
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Cowan
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002844:Chromatium / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000302:isolation & purification; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins; D011487:Protein Conformation
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D009587:Nitrogen Isotopes; D045322:Photosynthetic Reaction Center Complex Proteins; C007943:high potential iron-sulfur protein