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Published October 1978 | public
Journal Article

^(13)C nuclear magnetic resonance studies of the binding of isocyanides to various hemoglobins and myoglobins

Abstract

Interactions between ethyl and isopropyl isocyanides and various hemoglobins and myoglobins have been studied by ^(13)C nuclear magnetic resonance. The results indicate that the chemical shift of the bound isocyanide depends on the structure of the hemoglobin subunit or myoglobin. The resonances exhibited by isocyanides bound to myoglobin are sensitive to pH in contrast to the situation with rabbit and human hemoglobins. β subunits of opossum, rabbit, and human hemoglobins show a significantly greater preferential affinity for CO relative to EIC than do α subunits which have allowed the assignment of resonances. Rabbit, human, and opossum hemoglobin subunits bind ethyl isocyanide without observable preferences and an excess of DPG does not appear to affect this random order of ligation. In contrast, an excess of IHP seems to cause preferential ligation of the α subunits in these hemoglobins. The results have been used to gain insights into the differing characteristics of the ligand binding pockets of these various hemoglobins.

Additional Information

© 1978 American Chemical Society. Received May 24, 1977; revised manuscript received January 6, 1978. This work was supported by the National Institutes of Health Grants HL 15198, HL 15162, and GM 16424.

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023