Analysis of cooperativity in hemoglobin. Valency hybrids, oxidation, and methemoglobin replacement reactions.
An allosteric model proposed previously for structure-function relations in hemoglobin is applied to the analysis of low- and high-spin valency hybrids. By assuming that the low-spin oxidized chains have the tertiary structure of oxygenated chains while the high-spin oxidized chains have a tertiary structure intermediate between that of deoxygenated and oxygenated chains, the model parameters associated with the different valency hybrids can be obtained, and their equilibrium properties can be estimated. The hybrid results are used also to provide an interpretation of methemoglobin and its ligand replacement reactions and of the oxidation-reduction equilibrium of normal hemoglobin. For the various systems studied it is found that the effects of pH and 2,3-diphosphoglycerate are in agreement with the model.
D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D004163:Diphosphoglyceric Acids / Q000097:blood; D006454:Hemoglobins; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008024:Ligands; D046911:Macromolecular Substances; D008433:Mathematics; D008706:Methemoglobin; D008954:Models, Biological; D010084:Oxidation-Reduction; D010100:Oxygen / Q000097:blood; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D004163:Diphosphoglyceric Acids; D006454:Hemoglobins; D008024:Ligands; D046911:Macromolecular Substances; D008706:Methemoglobin; D010100:Oxygen