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 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.
|Original language||English (US)|
|Number of pages||4|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1976|
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