Bohr effect, hemoglobin function

This expression is called a linked function and indicates how the binding of ligands at nearby sites can influence each other. See also Basic Regulatory Kinetics Cooper-ativity Allosterism Feedback Effectors Bohr Effect Hemoglobin Le Chatelier s Principle Adair Equation... 

In order to achieve high concentrations of HCOj" from dissolved CO2, the resulting protons must be removed, i.e. accommodated by a buffer system. The principal buffers serving this function are plasma proteins (accounting for about 10% of the protons), erythrocyte phosphate (about 20%) and erythrocyte hemoglobin (60-70%). For the role of hemoglobin, see Bohr effect. Hemoglobin. 

When such an amino acid is incorporated into a protein, the local chemical environment in the protein may affect the pK of a group and thus alter its charge. Such changes can be very important in the function of proteins (e.g., the Bohr effect in hemoglobin depends on structural changes that affect the pK of histidine... 

In a recent study Chiancone et al. [469] investigate the Cl binding to the two main hemoglobin components in trout blood, Hb-Trout I and Hb-Trout IV. These two hemoglobins from the species Salmo irideus are electrophoretically different and may be separated. The two components have strikingly different functional properties. A Root effect (the equivalent of the Bohr effect for human hemoglobin),... 

The assumption that the dissociation of the two oxygen-linked acid groups are independent of each other is not necessary for a quantitative treatment of the Bohr effect. Alberty (1955) derived an expression of AX for the more general case where the dissociation of these two acid groups are not independent of each other. His expression has the same functional dependence on [H ] as Wyman s. In particular, for hemoglobin with K2IK1 1 and 1, Alberty s numerical results are... 

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