Kinetics of calcium release from manganese peroxidase during thermal inactivation

Archives of Biochemistry and Biophysics
S L Timofeevski, S D Aust

Abstract

It was previously reported that manganese peroxidase from the white-rot fungus Phanerochaete chrysosporium was susceptible to thermal inactivation because it contains relatively labile Ca2+ ions required for stability and activity [Sutherland and Aust (1996) Arch. Biochem. Biophys. 332, 128-134]. In this work we determined that four Ca2+ ions are present in the enzyme as isolated but this was reduced to 2 mol/mol upon treatment with Ca2+-chelating agents or extensive dialysis of dilute enzyme. One of two relatively tightly bound Ca2+ remaining in the enzyme was released during thermal inactivation at pH 7.2. Inactive enzyme contained one Ca2+ which could be removed in acidic conditions. Inactivation kinetics were biphasic and the rates for the two inactivation steps and the release of Ca2+ during inactivation suggested that the first, faster phase of inactivation was coupled to the removal of Ca2+. The weakly associated Ca2+ normally present in the enzyme did not affect enzyme activity and did not seem to protect the enzyme from thermal inactivation at submicromolar enzyme concentrations. Excess Ca2+ or Mn2+ decreased the rate of the thermal inactivation and Mn2+ stabilized the enzyme more efficiently than Ca2+ at higher temper...Continue Reading

References

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Citations

Feb 21, 2006·Biophysical Chemistry·Jorge VerdínRafael Vázquez-Duhalt
Jul 31, 2002·Biochimica Et Biophysica Acta·Ivan Yu Sakharov, Irina V Sakharova

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