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Molecules 2010, 15(5), 2935-2948; doi:10.3390/molecules15052935

Artificial Self-Sufficient P450 in Reversed Micelles

1
Department of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan
2
Center for NanoBio Integration, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan
3
Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan
4
Department of Applied Chemistry, Graduate School of Engineering & Center for Future Chemistry, Kyushu University, Motooka 744, Fukuoka 819-0395, Japan
5
New Energy and Industrial Technology Development Organization, 19F Muza Kawasaki Building, 1310, Omiya-cho, Saiwai-ku, Kawasaki City Kanagawa 212-8554, Japan
*
Author to whom correspondence should be addressed.
Received: 11 March 2010 / Revised: 14 April 2010 / Accepted: 23 April 2010 / Published: 27 April 2010
(This article belongs to the Special Issue Macromolecules: Chemistry, Medicinal and Functional Materials)
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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.
Keywords: artificial self-sufficient cytochrome P450; cofactor regeneration; transglutaminase; reversed micelles artificial self-sufficient cytochrome P450; cofactor regeneration; transglutaminase; reversed micelles
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MDPI and ACS Style

Hirakawa, H.; Kamiya, N.; Kawarabayasi, Y.; Nagamune, T. Artificial Self-Sufficient P450 in Reversed Micelles. Molecules 2010, 15, 2935-2948.

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