← Back to Search
CONTROL OF OXYGEN AFFINITY IN MAMMALIAM HEMOGLOBINS: Implications For A System Biology Description Of The Respiratory Properties Of The Red Blood Cell.
A. Bellelli, M. Brunori
Published 2020 · Biology, Medicine
Save to my Library
Download PDFAnalyze on Scholarcy
Hemoglobin and myoglobin have been considered for a long time the paradigmatic model systems for protein function, to the point of being defined the "hydrogen atom[s] of biology" [Frauenfelder et al. Proc. Natl. Acad. Sci. USA, 2003; 100, 8615-8617]. Given this privileged position and the huge amount of quantitative information available on these proteins, the red blood cell might appear as the model system and"hydrogen atom" of system biology. Indeed, since the red cell's main function is O2 transport by hemoglobin, the gap between the protein and the may appear quite small. Yet, a surprisingly large amount of detailed biochemical information is required for the modellization of the respiratory properties of the erythrocyte. This problem is compounded if modellization aims at uncovering or explaining evolutionarily selected functional properties of hemoglobin. The foremost difficulty lies in the fact that hemoglobins having different intrinsic properties and relatively ancient evolutionary divergence may behave similarly in the complex milieu of blood, whereas very similar hemoglobins sharing a substantial sequence similarity may present important functional differences because of the mutation of a few key residues. Thus the functional properties of hemoglobin and blood may reflect more closely the recent environmental challenges than the remote evolutionary history of the animal. We summarize in this review the case of hemoglobins from mammals, in an attempt to provide a reasoned summary of their complexity that, we hope, may be of help to scientists interested in the quantitative exploration of the evolutionary physiology of respiration. Indeed the basis of a meaningful modellization of the red cell requires a large amount of information collected in painstaking and often forgotten studies of the biochemical properties of hemoglobin carried out over more than a century.
This paper references
Non-Allosteric Cooperativity in Hemoglobin.
A. Bellelli (2018)
Purification and functional properties of the hemoglobin components from the rat (Wistar).
S. Condó (1981)
Interaction of hemoglobin with hydrogen ions, carbon dioxide, and organic phosphates.
J. Kilmartin (1973)
Chronic measurement of cardiac output in conscious mice.
B. Janssen (2002)
The reactions of the isolated alpha and beta chains of human hemoglobin with oxygen and carbon monoxide.
M. Brunori (1966)
Comparative study of the oxyhaemoglobin dissociation curve of four mammals: man, dog, horse and cattle.
T. Clerbaux (1993)
Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes.
A. Chanutin (1967)
A genetic mechanism for Tibetan high-altitude adaptation
F. Lorenzo (2014)
Cooperative interactions of hemoglobin.
S. Edelstein (1975)
Interstitial pH in human skeletal muscle during and after dynamic graded exercise
D. Street (2001)
The allosteric properties of hemoglobin: insights from natural and site directed mutants.
A. Bellelli (2006)
Molecular adaptation to physiological requirements: the hemoglobin system of trout.
M. Brunori (1975)
Functional characterisation of Eskimo dog hemoglobin: I. Interaction of Cl- and 2,3-DPG and its importance to oxygen unloading at low temperature.
A. Bårdgard (1997)
Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant.
S. Tomita (1971)
Allosteric Effects in Haemoglobin
K. Imai (1982)
Multiple structural genes for the α chain of canine (Canis familiaris) hemoglobin
S. L. Dresler (2004)
Oxygen dissociation curves of mammalian blood in relation to body size.
K. SCHMIDT-NEILSEN (1958)
Species adaptation in a protein molecule.
M. Perutz (1983)
The role of hemoglobin oxygen affinity in oxygen transport at high altitude
R. Winslow (2007)
Hemoglobin–oxygen affinity in high-altitude vertebrates: is there evidence for an adaptive trend?
J. F. Storz (2016)
Identification of residues contributing to the Bohr effect of human haemoglobin.
M. Perutz (1980)
A proton nuclear magnetic resonance investigation of the anion Bohr effect of human normal adult hemoglobin.
I. Russu (1989)
Blood and hemoglobin: The evolution of knowledge of functional adaptation in a biochemical system
J. Edsall (1972)
On the Measurement of Cooperativity and the Physico-Chemical Meaning of the Hill Coefficient.
A. Bellelli (2019)
Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions.
C. Fronticelli (1984)
Comparative genomics of canine hemoglobin genes reveals primacy of beta subunit delta in adult carnivores
S. Zaldívar-López (2017)
Assessment of roles of surface histidyl residues in the molecular basis of the Bohr effect and of beta 143 histidine in the binding of 2,3-bisphosphoglycerate in human normal adult hemoglobin.
T. Fang (1999)
Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins.
A. Riggs (1998)
Functional aspects of hemoglobin evolution in the mammals
A. Scott (2005)
Hemoglobin Polymorphism: Its Relation to Sickling of Erythrocytes in White-Tailed Deer
H. Kitchen (1964)
Cardiac Output in Horses
E. Fisher (1959)
Enthalpic consequences of reduced chloride binding in Andean frog (Telmatobius peruvianus) hemoglobin
R. Weber (2014)
The relationship between evolutionary and physiological variation in hemoglobin
R. Milo (2007)
Altered hemoglobin co-factor sensitivity does not underlie the evolution of derived fossorial specializations in the family Talpidae.
K. L. Campbell (2018)
Interaction of hemoglobin with salts. Effects on the functional properties of human hemoglobin.
G. Amiconi (1981)
The effect of pH and D-glycerate 2,3-bisphosphate on the O2 equilibrium of normal and SH(beta 93)-modified human hemoglobin.
E. Antonini (1982)
Adaptation to high altitude.
C. Lenfant (1971)
The Bohr effect of haemoglobin in vertebrates: an example of molecular adaptation to different physiological requirements.
B. Giardina (2004)
Factors in the evolution of hemoglobin function.
Austen Riggs (1976)
Synthetic Models for the Oxygen-Binding Hemoproteins
J. P. Collman (1977)
Hemoglobin and cooperativity: Experiments and theories.
A. Bellelli (2010)
A 35Cl(-)-NMR study of the singular anion-binding properties of dromedary hemoglobin.
P. Lundberg (1989)
Functional characterisation of Eskimo dog hemoglobin: II. The interplay of HCO(3)- and Cl-.
A. Bårdgard (1997)
How bar-headed geese fly over the Himalayas.
G. Scott (2015)
Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies.
M. Corda (2003)
The oxygen affinity of mammalian hemoglobins in the absence of 2,3-diphosphoglycerate in relation to body weight.
Nakashima Masae (1985)
Evolution of mammalian hemoglobin function.
H. Bunn (1981)
Red cell function at extreme altitude on Mount Everest.
R. Winslow (1984)
Effect of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus.
C. Bonaventura (1974)
Oxygen saturation and heart rate in healthy school children and adolescents living at high altitude
L. Huicho (2001)
Comparative studies of the respiratory functions of mammalian blood. IX. Ring-tailed lemur(Lemur catta)and black lemur (Lemur macaco).
D. S. Dhindsa (1972)
The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin.
R. Benesch (1967)
The Nature and Significance of the Bohr Effect in Mammalian Hemoglobins
Austen Riggs (1960)
Evidence for two oxygen-linked binding sites for polyanions in dromedary hemoglobin.
G. Amiconi (1985)
Variability of oxygen affinity of blood: human subjects native to high altitude.
R. Winslow (1981)
Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin.
A. Rażyńska (1990)
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
J. Monod (1965)
Hemoglobin function under extreme life conditions.
M. Clementi (1994)
Hemoglobin Polymerization in Mice
Austen Riggs (1965)
Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution.
V. Richard (1993)
Calorimetric studies of hemoglobin function, the binding of 2,3-diphosphoglycerate and inositol hexaphosphate to human hemoglobin A.
Dennis P. Nelson (1974)
Polymerization of Hemoglobins of Mouse and Man: Structural Basis
J. Bonaventura (1967)
Hemoglobins from Wistar rat: crystallization of components and intraerythrocytic crystals.
M. Brunori (1982)
Hemoglobin: Molecular, Genetic and Clinical Aspects
H. Bunn (1984)
Bohr effect and temperature sensitivity of hemoglobins from highland and lowland deer mice.
B. Jensen (2016)
Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata).
O. Brix (1990)
LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK.
J. Wyman (1964)
The effects of 2,3‐diphosphoglycerate on native and chemically modified horse hemoglobin
J. Salhany (1971)
Cat hemoglobin. pH dependence of cooperativity and ligand binding.
M. N. Hamilton (1974)
THE HEMOGLOBIN SYSTEM VI. THE OXYGEN DISSOCIATION CURVE OF HEMOGLOBIN
G. Adair (1925)
Enthalpic partitioning of the reduced temperature sensitivity of O2 binding in bovine hemoglobin.
R. E. Weber (2014)
Allosteric interpretation of haemoglobin properties.
R. Shulman (1975)
COMPARATIVE ANIMAL PHYSIOLOGY
C. Prosser (1950)
The Combinations of Haemoglobin with Oxygen and with Carbon Monoxide. I.
A. V. Hill (1913)
Allostery and cooperativity revisited
Q. Cui (2008)
Genetic differences in hemoglobin function between highland and lowland deer mice
J. F. Storz (2010)
STUDIES ON THE RELATIONS BETWEEN MOLECULAR AND FUNCTIONAL PROPERTIES OF HEMOGLOBIN. V. THE INFLUENCE OF TEMPERATURE ON THE BOHR EFFECT IN HUMAN AND IN HORSE HEMOGLOBIN.
E. Antonini (1965)
Predictable convergence in hemoglobin function has unpredictable molecular underpinnings
C. Natarajan (2016)
Myoglobin: The hydrogen atom of biology and a paradigm of complexity
H. Frauenfelder (2003)
Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
M. Perutz (1970)
Normal whole blood Bohr effect in Peruvian natives of high altitude.
R. Winslow (1985)
Different hematologic responses to hypoxia in Sherpas and Quechua Indians.
R. Winslow (1989)
The phylogenetic distribution of red cell 2,3 diphosphoglycerate and its interaction with mammalian hemoglobins.
A. Scott (1977)
Oxygen affinity and Bohr coefficients of dog blood.
R. B. Reeves (1982)
X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin
A. Arnone (1972)
Reduction of blood oxygen affinity in dogs by infusion of glycolytic intermediates.
J. D. Bristow (1977)
This paper is referenced by
Mismatch between Tissue Partial Oxygen Pressure and Near-Infrared Spectroscopy Neuromonitoring of Tissue Respiration in Acute Brain Trauma: The Rationale for Implementing a Multimodal Monitoring Strategy
Mario Forcione (2021)