Artificial Self-Sufficient P450 in Reversed Micelles

作者：Hirakawa Hidehiko; Kamiya Noriho; Kawarabayasi Yutaka; Nagamune Teruyuki^*

来源：Molecules, 2010, 15(5): 2935-2948.

DOI：10.3390/molecules15052935

• artificial self-sufficient cytochrome P450
• cofactor regeneration
• transglutaminase
• reversed micelles

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.

• 出版日期2010-5