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. 1976 Mar;73(3):800–803. doi: 10.1073/pnas.73.3.800

Linearity of the hemoglobin oxidation bohr effect.

B M Hoffman, C Bull
PMCID: PMC336006  PMID: 1062790

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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