Activation of Wild-Type Cytochrome P450BM3 by the Next Generation of Decoy Molecules: Enhanced Hydroxylation of Gaseous Alkanes and Crystallographic Evidence

Zhiqi Cong, Osami Shoji, Chie Kasai, Norifumi Kawakami, Hiroshi Sugimoto, Yoshitsugu Shiro, Yoshihito Watanabe

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

The direct hydroxylation of alkanes under mild conditions is a key issue in catalytic chemistry that addresses an increasing number of industrial and economic requirements. Cytochrome P450s are monooxygenases that are capable of oxidizing less reactive C-H bonds; however, wild-type P450s are unavailable for many important nonnative substrates such as gaseous alkanes. Here, we report the enhanced hydroxylation activities and crystallographic evidence for the role of decoy molecules in wild-type P450BM3-catalyzed hydroxylation of gaseous ethane and propane by using the next generation of decoy molecule. A cocrystal structure of P450BM3 and a decoy molecule reveals that an N-perfluoroacyl amino acid (decoy molecule) partially occupies the substrate-binding site of P450BM3. This binding of the decoy re-forms the active site pocket to allow the accommodation of small substrates and simultaneously influences the formation of compound I species by expelling water molecules from the active site. (Chemical Equation Presented).

Original languageEnglish
Pages (from-to)150-156
Number of pages7
JournalACS Catalysis
Volume5
Issue number1
DOIs
Publication statusPublished - 2015 Jan 2
Externally publishedYes

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Keywords

  • biocatalysis
  • cytochromes
  • decoy molecule
  • gaseous alkanes
  • hydroxylation

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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