Cooperative hydrogen ligand binding inducing the Bohr effect in human hemoglobin. A general methodology.
A cooperative model applied to hydrogen ligand binding curves of normal human hemoglobin indicates that the Bohr effect is a cooperative (n) change rather than a pK shift. The analysis suggests a molecular mechanism whose energetic justification acquires a specific physiological significance.
Dipartimento di Medicina Sperimentale, Facolta' di Medicina, Universita' La Sapienza, Rome, Italy.
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Forlani
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Marini
D001665:Binding Sites; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008956:Models, Chemical; D015394:Molecular Structure; D010108:Oxyhemoglobins / Q000737:chemistry; D011522:Protons; D013816:Thermodynamics
D006454:Hemoglobins; D008024:Ligands; D010108:Oxyhemoglobins; D011522:Protons; C100003:deoxyhemoglobin