Studies on the enantioselective oxidation of β-ionone with a whole E. coli system expressing cytochrome P450 monooxygenase BM3

D Zehentgruber, VB Urlacher, S Lütz

Index: Zehentgruber, Daniela; Urlacher, Vlada B.; Luetz, Stephan Journal of Molecular Catalysis B: Enzymatic, 2012 , vol. 84, p. 62 - 64

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Citation Number: 7

Abstract

Recombinant Escherichia coli cells, expressing an NADH-dependent cytochrome P450 monooxygenase BM-3 mutant, were used for the hydroxyalation of the sesquiterpenoid β- ionone to (R)-4-hydroxy-β-ionone. The decrease in enantioselectivity of cytochrome P450 monooxygenase BM-3 catalyzed hydroxylation of β-ionone can be ascribed to the overoxidation of the desired product. In this initial study we report, that by addressing ...