title: The Nernst equation applied to oxidation-reduction reactions in myoglobin and hemoglobin. Evaluation of the parameters.
abstract: Analyses of the binding of oxygen to monomers such as myoglobin employ the Mass Action equation. The Mass Action equation, as such, is not directly applicable for the analysis of the binding of oxygen to oligomers such as hemoglobin. When the binding of oxygen to hemoglobin is analyzed, models incorporating extensions of mass action are employed. Oxidation-reduction reactions of the heme group in myoglobin and hemoglobin involve the binding and dissociation of electrons. This reaction is described with the Nernst equation. The Nernst equation is applicable only to a monomeric species even if the number of electrons involved is greater than unity. To analyze the oxidation-reduction reaction in a molecule such as hemoglobin a model is required which incorporates extensions of the Nernst equation. This communication develops models employing the Nernst equation for oxidation-reduction reactions analogous to those employed for hemoglobin in the analysis of the oxygenation (binding of oxygen) reaction.
authors.affiliation: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. saroff@helix.nih.gov
authors.forename: Harry A
authors.initials: HA
authors.lastname: Saroff
mesh_terms: D001665:Binding Sites; D019281:Dimerization; D006454:Hemoglobins / Q000737:chemistry*; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D009211:Myoglobin / Q000737:chemistry*; D010084:Oxidation-Reduction
chemical_list: D006454:Hemoglobins; D008024:Ligands; D009211:Myoglobin