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Artificial Self-Sufficient P450 in Reversed Micelles
AbstractCytochrome 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.
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Hirakawa, H.; Kamiya, N.; Kawarabayasi, Y.; Nagamune, T. Artificial Self-Sufficient P450 in Reversed Micelles. Molecules 2010, 15, 2935-2948.View more citation formats
Hirakawa H, Kamiya N, Kawarabayasi Y, Nagamune T. Artificial Self-Sufficient P450 in Reversed Micelles. Molecules. 2010; 15(5):2935-2948.Chicago/Turabian Style
Hirakawa, Hidehiko; Kamiya, Noriho; Kawarabayasi, Yutaka; Nagamune, Teruyuki. 2010. "Artificial Self-Sufficient P450 in Reversed Micelles." Molecules 15, no. 5: 2935-2948.
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