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Oxygenation of Nonnative Substrates Using a Malfunction State of Cytochrome P450s

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Fifty Years of Cytochrome P450 Research

Abstract

The substrate specificity of bacterial cytochrome P450s is very high. Therefore, their catalytic activities toward nonnative substrates are low, whereas their inherent catalytic activities are very high compared with P450s isolated from animals and plants. Using “decoy” molecules, whose structures are very similar to natural substrates, to trick their substrate recognition with decoy molecules, we can induce a malfunction state of cytochrome P450s. Decoy molecule binding under this malfunction state allows bacterial cytochrome P450s to catalyze the oxidation reaction of nonnative substrates. This system using decoy molecules does not require any substitution of amino acids to alter substrate specificity or any changes in the enantioselectivity of nonnative substrate oxidation.

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Acknowledgments

This work was supported by Grants-in-Aid for Scientific Research (S) to Y.W. (24225004) and a Grant-in-Aid for Young Scientists (A) to O.S. (21685018) from the Ministry of Education, Culture, Sports, Science, and Technology (Japan).

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Authors and Affiliations

  1. Department of Chemistry, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan

    Osami Shoji

  2. Research Center for Materials Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan

    Yoshihito Watanabe

Authors
  1. Osami Shoji
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  2. Yoshihito Watanabe
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Correspondence to Osami Shoji .

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Editors and Affiliations

  1. Showa Pharmaceutical University, Tokyo, Japan

    Hiroshi Yamazaki

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Shoji, O., Watanabe, Y. (2014). Oxygenation of Nonnative Substrates Using a Malfunction State of Cytochrome P450s. In: Yamazaki, H. (eds) Fifty Years of Cytochrome P450 Research. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54992-5_6

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