Abstract
A fluorine NMR study of cyanomethemoglobin prepared from hemoglobin isolated from rabbits maintained on a diet containing DL-p-fluorophenylalanine is described. The results indicate that substitution of fluorophenylalanine occurs essentially randomly at all phenylalanine positions of the alpha- and beta-globin chains; a set of hybrid hemoglobins in which only the alpha- or only the beta-chains contain the fluorinated amino acid was prepared and used to ascertain the fluorine NMR signals arising from each chain. The temperature and pH dependences of chemical shifts, spin-lattice relaxation times, 19F(1H) nuclear Overhauser effects, and the effect of chemical modification of the beta-93 sulfhydryl groups were examined. When considered in light of presently available X-ray structures of human and horse hemoglobins, the available data permit a tentative assignment of most signals to particular fluorophenylalanine/phenylalanine positions in the globin sequences.
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