Use of apomyoglobin to gently remove heme from a H2O2-dependent cytochrome P450 and allow its reconstitution

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Abstract

The heme of hydrogen peroxide-dependent cytochrome P450BSβ (P450BSβ) was removed by apomyoglobin under mild conditions to give apo-P450BSβ without the need for acidic conditions and organic solvents. The circular dichroism spectrum of the apo-P450BSβ was essentially identical to that of holo-P450BSβ, showing a small structural change resulting from the removal of heme using apomyoglobin. The apo-P450BSβ was reconstituted with hemin or manganese protoporphyrin IX (MnPPIX), and the resulting reconstituted P450BSβ catalyzed the one-electron oxidation of guaiacol using hydrogen peroxide as an oxidant. A higher catalytic activity was observed for P450BSβ reconstituted with MnPPIX when meta-chloroperoxybenzoic acid (mCPBA) was used as the oxidant.

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Chien, S. C., Shoji, O., Morimoto, Y., & Watanabe, Y. (2016). Use of apomyoglobin to gently remove heme from a H2O2-dependent cytochrome P450 and allow its reconstitution. New Journal of Chemistry, 41(1), 302–307. https://doi.org/10.1039/c6nj02882a

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