Linearity of the hemoglobin oxidation bohr effect.

AUTOR(ES)

Hoffman, B M

RESUMO

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.

Documentos Relacionados

• Interaction of hemoglobin with three ligans: organic phosphates and the Bohr effect.
• Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin.
• Direct Measurement of the pK Values of an Alkaline Bohr Group in Human Hemoglobin
• On the mechanism of the modular primer effect.
• Red pepper effect.