pH-Linked Binding of Mn(II) to Manganese Peroxidase

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Abstract
The stability of Mn(II) binding to manganese peroxidase (MnP) has been studied as a function of pH by spectrophotometric and potentiometric titrations. The sensitivity of the potentiometric titrations allows collection of data that are consistent with a high-affinity and a low-affinity Mn(II) binding site on the peroxidase. The two sites differ in affinity by 4 to 900-fold between pH 4 and 6.5. The stability of Mn(II) binding to the high-affinity site increases with increasing pH, while the stability of Mn(II) binding to the low-affinity site decreases with increasing pH. Interestingly, at pH values above 5.0, the high-affinity site appears to be partially unavailable for binding Mn(II). A pH-dependent structural change in the Mn(II) binding site is proposed to account for this partial inactivation at elevated pH.

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