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Issue 1, 2017
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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.

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

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Publication details

The article was received on 16 Sep 2016, accepted on 21 Nov 2016 and first published on 22 Nov 2016


Article type: Paper
DOI: 10.1039/C6NJ02882A
Citation: New J. Chem., 2017,41, 302-307
  • Open access: Creative Commons BY license
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    Use of apomyoglobin to gently remove heme from a H2O2-dependent cytochrome P450 and allow its reconstitution

    S. Chien, O. Shoji, Y. Morimoto and Y. Watanabe, New J. Chem., 2017, 41, 302
    DOI: 10.1039/C6NJ02882A

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