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Published April 1978 | public
Journal Article

Spectroscopic studies of the nature of ligand bonding in carbonmonoxyhemoglobins: evidence of a specific function for histidine-E7 from infrared and nuclear magnetic resonance intensities

Abstract

Infrared spectra of carbon monoxide ligated hemoglobins from human, horse, and rabbit donors have been examined. A single vibrational frequency at 1951 cm^(-1) is observed for CO bound to the heme in horse and human hemoglobins. Studies of the isolated α-CO and β -CO subunits of human hemoglobin reveal that the observation of a single frequency in the intact tetramer is the result of a superposition of the α-CO and β-CO vibrational frequencies. The apparent integrated absorption intensities of these CO vibrations are shown both to have values of 1.0 X 10^5 M^(-1) cm^(-2) within experimental error. For rabbit CO-Hb two vibrational frequencies appear (Caughey, W. S., et al. (1973) Fed. Proc., Fed. Am. Soc. Exp. Biol. 32, 552) and are assigned to CO bound to the β (1951 cm^(-1)) and a (1928 cm^(-1)) subunits within the intact tetramer. The β-CO subunit exhibits both frequency and intensity similarities with horse and human hemoglobins. The rabbit α-CO subunit, however, exhibits a markedly lower frequency and much smaller intensity compared with the other CO-hemoglobins. These data are interpreted in terms of a specific role for the distal histidine (E7) in rabbit a subunits, in which this histidine functions as a nucleophilic donor to coordinated CO.

Additional Information

© 1978 American Chemical Society. Received April 25, 1977. This work was supported by National Institutes of Health Grants HL 15162, HL 15198, and GM-16424. The authors are indebted to Professor G. N. La Mar for the gift of equine blood and to Professor H. B. Gray for valuable discussions.

Additional details

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