Thermodynamics of oxygen binding to arctic hemoglobins. The case of reindeer.

Details

Serval ID
serval:BIB_62721C598FCB
Type
Article: article from journal or magazin.
Collection
Publications
Title
Thermodynamics of oxygen binding to arctic hemoglobins. The case of reindeer.
Journal
Biophysical Chemistry
Author(s)
Giardina B., Condò S.G., Petruzzelli R., Bardgard A., Brix O.
ISSN
0301-4622 (Print)
ISSN-L
0301-4622
Publication state
Published
Issued date
1990
Peer-reviewed
Oui
Volume
37
Number
1-3
Pages
281-286
Language
english
Abstract
The most surprising characteristic of reindeer hemoglobin (Hb) concerns its response to changes in temperature. Thus, the shape of the oxygen-binding curve is strongly temperature dependent due to the difference in the enthalpy of oxygenation between the T and R state of the molecule. In fact, delta H of oxygen binding to the T state is strongly exothermic whereas that of the R state is very close to zero or possibly positive after correction for the heat of oxygen solubilization. Moreover, the allosteric transition T0----R0 has been found to display a negative delta H and a contemporaneous decrease in entropy, a behavior which is precisely the opposite of what has been reported for other hemoglobins. As a whole, reindeer Hb represents a beautiful example of the significance that comparative studies may have in assessing the general validity of the main properties of the hemoglobin molecule.
Keywords
2,3-Diphosphoglycerate, Animals, Arctic Regions, Diphosphoglyceric Acids/metabolism, Hemoglobin A/metabolism, Hemoglobins/metabolism, Humans, Hydrogen-Ion Concentration, Kinetics, Mathematics, Models, Theoretical, Oxyhemoglobins/metabolism, Protein Conformation, Reindeer/blood, Thermodynamics
Pubmed
Web of science
Create date
03/08/2014 13:35
Last modification date
20/08/2019 14:19
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