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

Dill, Kilian and Satterlee, James D. and Richards, John H. (1978) ^(13)C nuclear magnetic resonance studies of the binding of isocyanides to various hemoglobins and myoglobins. Biochemistry, 17 (20). pp. 4291-4298. ISSN 0006-2960. https://resolver.caltech.edu/CaltechAUTHORS:20150505-103739032

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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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00613a028DOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi00613a028PublisherArticle
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.
Funders:
Funding AgencyGrant Number
NIHHL 15198
NIHHL 15162
NIHGM 16424
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Caltech Church Laboratory of Chemical Biology5498
Issue or Number:20
Record Number:CaltechAUTHORS:20150505-103739032
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150505-103739032
Official Citation:13C nuclear magnetic resonance studies of the binding of isocyanides to various hemoglobins and myoglobins Kilian Dill, James D. Satterlee, and John H. Richards Biochemistry 1978 17 (20), 4291-4298 DOI: 10.1021/bi00613a028
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57227
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:05 May 2015 19:30
Last Modified:03 Oct 2019 08:22

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