Abstract
The hydrogen ion titration curves of horse cyanometmyoglobin and metmyoglobin have been measured between pH 5.5 and 9.5. The most likely explanation of the titration results of cyanometmyoglobin is that 6 histidines are titratable with an intrinsic pK of 6.8 and an electrostatic interaction factor w of 0.150; in addition the results indicate that the total number of titratable carboxyl groups is 25, two more than calculated from the covalent structure of horse myoglobin. The titration behavior of metmyoglobin is explicable assuming the presence of one extra group as compared to cyanometmyoglobin with a pK near 9, which contributes to the maximum positive charge.
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