Artificial self-sufficient P450 in reversed micelles

Molecules. 2010 Apr 27;15(5):2935-48. doi: 10.3390/molecules15052935.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Dehydrogenase
  • Cross-Linking Reagents
  • Cytochrome P-450 Enzyme System / chemistry*
  • Electron Transport*
  • Micelles*
  • Protein Engineering / methods*
  • Recombinant Fusion Proteins

Substances

  • Cross-Linking Reagents
  • Micelles
  • Recombinant Fusion Proteins
  • Cytochrome P-450 Enzyme System
  • Alcohol Dehydrogenase