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Alkene epoxidation catalyzed by cytochrome P450 BM-3 139-3 Edgardo T. Farinas,
 

Summary: Alkene epoxidation catalyzed by cytochrome P450 BM-3 139-3
Edgardo T. Farinas,
Miguel Alcalde
and Frances Arnold*
Division of Chemistry and Chemical Engineering, California Institute of Technology, 210-41, Pasadena, CA 91125, USA
Received 20 June 2003; accepted 17 October 2003
Abstract--We recently reported conversion of cytochrome P450 BM-3, a medium-chain (C12 C18) fatty acid monooxygenase, into a highly
efficient alkane hydroxylase by directed evolution [Nat. Biotechnol. 2002, 20, 1135]. P450 BM-3 mutant 139-3 exhibited high activity
towards a variety of fatty acid and alkane substrates, including C3C8 alkanes. We report here that mutant 139-3 is also active on benzene,
styrene, cyclohexene, 1-hexene, and propylene. Benzene is converted to phenol, while styrene is converted to styrene oxide. Propylene
oxidation generates only propylene oxide, but cyclohexene oxidation produces a mixture of cyclohexene oxide (85%) and 2-cyclohexene-1-
ol (15%), and 1-hexene is converted to the allylic hydroxylation product, 1-hexene-3-ol. Initial rates of NADPH oxidation for 139-3 in the
presence of the substrates greatly (17- to .100-fold) surpass the wild-type in all cases. However, NADPH consumption is only partially
coupled to product formation (1479%). This cytochrome P450 epoxidation catalyst is a suitable starting point for further evolution to
improve coupling and activity.
q 2003 Elsevier Ltd. All rights reserved.
1. Introduction
Catalyzing a wide range of oxidative reactions under mild
conditions in aqueous solutions, cytochrome P450 mono-
oxygenases (P450s) are interesting potential `green' cata-

  

Source: Arnold, Frances H. - Division of Chemistry and Chemical Engineering, California Institute of Technology

 

Collections: Chemistry; Biology and Medicine