Artificial self-sufficient P450 in reversed micelles

Hidehiko Hirakawa, Noriho Kamiya, Yutaka Kawarabayasi, Teruyuki Nagamune

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Cytochrome P450s are heme-containing monooxygenases that require electron transfer proteins for their catalytic activities. They prefer hydrophobic compounds as substrates and it is, therefore, desirable to perform their reactions in non-aqueous media. Reversed micelles can stably encapsulate proteins in nano-scaled water pools in organic solvents. However, in the reversed micellar system, when multiple proteins are involved in a reaction they can be separated into different micelles and it is then difficult to transfer electrons between proteins. We show here that an artificial self-sufficient cytochrome P450, which is an enzymatically crosslinked fusion protein composed of P450 and electron transfer proteins, showed micelle-size dependent catalytic activity in a reversed micellar system. Furthermore, the presence of thermostable alcohol dehydrogenase promoted the P450-catalyzed reaction due to cofactor regeneration.

Original languageEnglish
Pages (from-to)2935-2948
Number of pages14
JournalMolecules
Volume15
Issue number5
DOIs
Publication statusPublished - May 1 2010

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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  • Cite this

    Hirakawa, H., Kamiya, N., Kawarabayasi, Y., & Nagamune, T. (2010). Artificial self-sufficient P450 in reversed micelles. Molecules, 15(5), 2935-2948. https://doi.org/10.3390/molecules15052935