Artificial self-sufficient P450 in reversed micelles.

Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry
Hidehiko HirakawaTeruyuki Nagamune

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.

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Citations

May 12, 2017·Nano Convergence·Teruyuki Nagamune

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Methods Mentioned

BETA
hydroxylation
gel-filtration

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