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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

Satterlee, James D. and Teintze, Martin and Richards, John H. (1978) 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. Biochemistry, 17 (8). pp. 1456-1462. ISSN 0006-2960. https://resolver.caltech.edu/CaltechAUTHORS:20150505-141849896

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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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00601a015DOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi00601a015PublisherArticle
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.
Funders:
Funding AgencyGrant Number
NIHHL 15162
NIHHL 15198
NIHGM-16424
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Caltech Church Laboratory of Chemical Biology5559
Issue or Number:8
Record Number:CaltechAUTHORS:20150505-141849896
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150505-141849896
Official Citation: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 James D. Satterlee, Martin Teintze, and John H. Richards Biochemistry 1978 17 (8), 1456-1462 DOI: 10.1021/bi00601a015
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57243
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:06 May 2015 16:37
Last Modified:03 Oct 2019 08:22

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