Monooxygenation of Nonnative Substrates Catalyzed by Bacterial Cytochrome P450s Facilitated by Decoy Molecules

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Author(s)

    • Shoji Osami
    • Department of Chemistry, Graduate School of Science, Nagoya University|Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency

Abstract

<p>Cytochrome P450s are a family of heme-containing enzymes that catalyze monooxygenation of inert substrates. Bacterial cytochrome P450s are great candidates as biocatalysts for synthetic applications because of their high hydroxylation activity and their high solubility in water. However, the substrate specificity of bacterial cytochrome P450s is generally high, and their low catalytic activities toward nonnative substrates tends to restrict their application as biocatalysts. We have developed a reaction system that utilizes dummy substrates with structures similar to those of natural substrates, as "decoy molecules". The decoy molecules induce substrate misrecognition of bacterial P450s, leading to the generation of the active species and ultimately enabling them to catalyze the oxidation of nonnative substrates. The catalytic activity and the enantioselectivity are dependent on the structure of the decoy molecules, suggesting that the reactions can be controlled by variation in the designed structure of the decoy molecules.</p>

Journal

  • Chemistry Letters

    Chemistry Letters 46(3), 278-288, 2017

    The Chemical Society of Japan

Codes

  • NII Article ID (NAID)
    130005436531
  • Text Lang
    ENG
  • ISSN
    0366-7022
  • Data Source
    J-STAGE 
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