Linearity of the hemoglobin oxidation bohr effect.
The hemoglobin oxidation Bohr effect below pH 7 is essentially proportional to the fraction of hemes oxidized, just as the ligation Bohr effect is proportional to fractional heme ligation. The reported nonlinear proton release during oxidation [(1965) J. Biol. Chem. 240, 3317-3324] is shown to be an artifact resulting from the use of ferricyanide as oxidant. Published forms of the two-state allosteric transition model for hemoglobin function have used several proton linkage schemes, and none are compatible with a linear proton release upon oxidation.
D006418:Heme / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D008954:Models, Biological; D010084:Oxidation-Reduction; D011522:Protons
D006454:Hemoglobins; D011522:Protons; D006418:Heme