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A synthetic cytochrome c peroxidase was reconstituted from apoenzyme and manganese protoporphyrin IX. The manganese enzyme was crystallized by dialysis against distilled water. The Mn enzyme formed well defined complexes with fluoride and azide. However, neither the Mn enzyme nor its dithionite-reduced compound formed complexes with CO and cyanide. The Mn enzyme was allowed to react with hydroperoxide to form a relatively stable peroxide compound which exhibited an intense electron paramagnetic resonance absorption of a free radical type at g = 2.003. The Mn enzyme and its derivatives thus far examined showed no electron paramagnetic resonance absorption attributable to Mn at -196°. The Mn enzyme catalyzed the peroxidatic oxidation of ferrocyanide, ferrocytochrome c, and ascorbate at reasonable rates.
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Yonetani et al. (1968) studied this question.
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