Hemoglobin function under extreme life conditions
Open Access
- 1 July 1994
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 223 (2) , 309-317
- https://doi.org/10.1111/j.1432-1033.1994.tb18996.x
Abstract
Considering the variety of species that depend on hemoglobin for oxygen transport, these molecules must execute their primary function under extreme environmental conditions. Hence, a thermodynamic analysis of oxygen binding with hemoglobins from different species reveals a series of adaptive mechanisms which are based on the thermodynamic connection between the binding of heterotropic effectors and the reaction with oxygen. The examples reported, from fishes to human fetus, illustrate how evolution can alter the structural basis of the heterotropic interactions to optimize the oxygenation-deoxygenation cycle in dependence of the physiological needs of the particular organisms. Moreover they show that a thermodynamic analysis of the reaction with oxygen overcomes the meaning of a detailed structural and functional characterization going deeper into the physiology of the specific organism.Keywords
This publication has 40 references indexed in Scilit:
- Adaptation to Extreme Environments: Structure-Function Relationships in Emperor Penguin HaemoglobinJournal of Molecular Biology, 1994
- Physiological Relevance of the Overall ΔH of Oxygen Binding to Fetal Human HemoglobinJournal of Molecular Biology, 1993
- Reduced sensitivity of O2 transport to allosteric effectors and temperature in loggerhead sea turtle hemoglobin: functional and spectroscopic studyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
- The primary structure of hemoglobin from reindeer (Rangifer tarandus tarandus) and its functional implicationsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Flight and heat dissipation in birdsFEBS Letters, 1990
- Arctic adaptation in reindeer The energy saving of a hemoglobinFEBS Letters, 1989
- High-Altitude Respiration of Geese. The Primary Structures of the Major and Minor Hemoglobin-Components of Adult Andean Goose (Chloephaga melanoptera, Anatidae): the Mutation Leu → Ser in Position 55 of the ß-ChainsBiological Chemistry Hoppe-Seyler, 1987
- Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus)Journal of Molecular Biology, 1983
- Different effects of 2.3 diphosphoglycerate and adenosine triphosphate on the oxygen affinity of adult and foetal human haemoglobinLife Sciences, 1968
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965