Linearity of the hemoglobin oxidation bohr effect - PubMed (original) (raw)
Linearity of the hemoglobin oxidation bohr effect
B M Hoffman et al. Proc Natl Acad Sci U S A. 1976 Mar.
Abstract
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.
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