The oxidation of hæmoglobin to methæmoglobin by oxygen

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Abstract
The decrease of Hb concn. in diluted blood containing dissolved O2 was due to the formation of methemoglobin. The oxidation of Hb to methemoglobin was, within the experimental limits, monomolecular with respect to the concn. of Hb. The rate of oxidation varied in different samples of blood. Decrease of pH increased the rate of oxidation. The rate was directly proportional to a power of the H-ion activity. With 3 different bloods the value of the power was 0.54, 0.54 and 0.61. The unconnected temp. coefficient was approximately 4 over the pH (18[degree] C.) range 5.72-7.06. The correction for the difference in concn. of dissolved O2 at the 2 temps. was unknown. Increase of the concn. of phosphate at pH 6.29 from 0.2 to 0.6 M increased the rate of oxidation by 19%; increase from 0.6 to 1.0 M had no further effect. An unknown fraction of the increase must be attributed to a decrease in the concn. of dissolved O2. Dissolved toluene had no effect on the rate of oxidation in concentrated salt solns. The presence of considerable amounts of liquid toluene changed the course of the reaction.

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