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Nuclear magnetic resonance studies of the phenylalanine residues of eukaryotic cytochrome c
Authors:A P Boswell  G R Moore  R J Williams  J C Chien  L C Dickinson
Affiliation:Inorganic Chemistry Laboratory, University of Oxford U.K.;Department of Chemistry, University of Massachusetts U.S.A.
Abstract:The resonances of Phe 82 and Phe 10 in the nuclear magnetic resonance spectra of horse cytochrome c are reassigned using nuclear Overhauser enhancements. The reassignments provide new information about the oxidation state linked conformation change of cytochrome c. The region of the protein now known to be affected by the change extends to the part of the protein close to Phe 10.
Keywords:Address reprint requests to: G.R. Moore   Inorganic Chemistry Laboratory   University of Oxford   South Parks Road   Oxford OX1 3QR   UK
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