Redox equilibria of liganded forms of methemoglobin.
We have examined the redox equilibria of azidomethemoglobin (low-spin) and fluoromethemoglobin (high-spin). We have derived a modified Hill equation which includes the tetramer--dimer equilibrium of the oxidized form, and also generalized the two-state model to incorporate ligand binding to the ferriheme. The pH dependence of the redox Hill's constant for fluoromethemoglobin is the same as that for methemoglobin, demonstrating that this dependence and the marked cooperativity achieved (n = 2.2) are not coupled to changes of the ferriheme spin state. The redox Hill's constant for azidomethemoglobin, however, is as large as the oxygenation Hill's constant (n approximately 2.7) and is also roughly pH independent.
D001665:Binding Sites; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008706:Methemoglobin / Q000378:metabolism*; D010084:Oxidation-Reduction; D010710:Phosphates / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D008024:Ligands; D010710:Phosphates; D008706:Methemoglobin