The reactivity of the heme iron is important in the function of the heme protein as well as the interaction between the heme cofactor and the surrounding protein. In our research, we determine the reduction potentials of the protein in the presence of fluoride. We have studied heme proteins such as myoglobin (Mb), hemoglobin (Hb), and horseradish peroxidase (HRP). In our recent study, we performed UV/Vis spectroelectrochemistry on the heme-bound fluoride complex of HRP-F. Upon comparison, the pH profiles of the reduction potentials of HRP and Mb in the presence of fluoride (Mb-F) are different. Specifically, the reduction potential of HRP-F increases at pH below 6, while that of Mb-F decreases. The difference in the trends of both these heme proteins at low pH is explained on the basis of the respective structural changes that occur in the heme cavity of each of these proteins.

Determination of the reduction potential of heme-bound fluoride complexes of horseradish peroxidase as a function of pH

247th National Meeting (2014)

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