Meso-unsubstituted iron corrole in hemoproteins: remarkable differences in effects on peroxidase activities between myoglobin and horseradish peroxidase

…, A Hayashi, M Abe, T Matsuda, Y Hisaeda…

Index: Matsuo, Takashi; Hayashi, Akihiro; Abe, Masato; Matsuda, Takaaki; Hisaeda, Yoshio; Hayashi, Takashi Journal of the American Chemical Society, 2009 , vol. 131, # 42 p. 15124 - 15125

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Citation Number: 36

Abstract

Myoglobin (Mb) and horseradish peroxidase (HRP) were both reconstituted with a meso- unsubstituted iron corrole and their electronic configurations and peroxidase activities were investigated. The appearance of the 540 nm band upon incorporation of the iron corrole into apoMb indicates axial coordination by the proximal histidine imidazole in the Mb heme pocket. Based on 1H NMR measurements using the Evans method, the total magnetic ...