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Issue 3, 2012
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P450BM3 (CYP102A1): connecting the dots

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Abstract

P450BM3 (CYP102A1), a fatty acid hydroxylase from Bacillus megaterium, has been extensively studied over a period of almost forty years. The enzyme has been redesigned to catalyse the oxidation of non-natural substrates as diverse as pharmaceuticals, terpenes and gaseous alkanes using a variety of engineering strategies. Crystal structures have provided a basis for several of the catalytic effects brought about by mutagenesis, while changes to reduction potentials, inter-domain electron transfer rates and catalytic parameters have yielded functional insights. Areas of active research interest include drug metabolite production, the development of process-scale techniques, unravelling general mechanistic aspects of P450 chemistry, methane oxidation, and improving selectivity control to allow the synthesis of fine chemicals. This review draws together the disparate research themes and places them in a historical context with the aim of creating a resource that can be used as a gateway to the field.

Graphical abstract: P450BM3 (CYP102A1): connecting the dots

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Publication details

The article was received on 18 Jul 2011 and first published on 18 Oct 2011


Article type: Critical Review
DOI: 10.1039/C1CS15192D
Citation: Chem. Soc. Rev., 2012,41, 1218-1260
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    P450BM3 (CYP102A1): connecting the dots

    C. J. C. Whitehouse, S. G. Bell and L. Wong, Chem. Soc. Rev., 2012, 41, 1218
    DOI: 10.1039/C1CS15192D

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