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15N resonance assignments of oxidized and reducedChromatium vinosum high-potential iron protein
Authors:Dawei Li  Charles E Cottrell  J A Cowan
Institution:1. Evans Laboratory of Chemistry, Ohio State University, 43210, Columbus, Ohio
Abstract:The15N resonances in reduced and oxidizedChromatium vinosum high-potential iron protein have been assigned by use of1H-1H COSY spectra and1H-15N HMQC, HMQC-COSY, and HMQC-NOESY spectra. Unambiguous assignment of 70 of 85 backbone15N resonances in the reduced protein and 62 of 85 resonances in the oxidized protein are made, as are 12 of 21 side-chain15N resonances.
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