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pubmed-article:9578561pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:9578561pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:9578561pubmed:articleTitlepH-linked binding of Mn(II) to manganese peroxidase.lld:pubmed
pubmed-article:9578561pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.lld:pubmed
pubmed-article:9578561pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9578561pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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