Magnetization Studies of the Reduced Active Form of the Catalase from Thermus thermophilus

摘要

Manganese-containing catalases are found in various bacteria such as Thermits thermophilus and Lactobacillus planturum. Structural and spectroscopic evidence indicate that the enzyme from T. thermophilus possesses a dimanganese active site, which exists in four different redox forms. Mechanistic studies have concluded that during catalysis the dimanganese center shuttles between a Mn~(II)Mn~(II) and a Mn~(III)Mn~(III) form. In vitro, mixed-valent forms Mn~(II)Mn~(III) and Mn~(III)Mn~(IV) can be generated.