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Manganese catalase binuclear structure

Catalases catalyze the conversion of hydrogen peroxide to dioxygen and water. Two families of catalases are known, one having a heme cofactor and the second a structurally distinct family, found in thermophilic and lactic acid bacteria. The manganese enzymes contain a binuclear active site and the functional form of the enzyme cycles between the (Mn )2 and the (Mn )2 oxidation states. When isolated, the enzyme is in a mixture of oxidation states including the Mn /Mn superoxidized state and this form of the enzyme has been extensively studied using XAS, UV-visible, EPR, and ESEEM spectroscopies. Multifrequency EPR and microwave polarization studies of the (Mn )2 catalytically active enzyme from L. plantarum have also been reported. ... [Pg.100]


See other pages where Manganese catalase binuclear structure is mentioned: [Pg.325]    [Pg.389]    [Pg.412]    [Pg.325]    [Pg.389]    [Pg.412]    [Pg.129]    [Pg.323]    [Pg.326]    [Pg.368]    [Pg.323]    [Pg.326]    [Pg.368]   
See also in sourсe #XX -- [ Pg.325 , Pg.326 ]




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