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Issue 15, 2017
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Control of stereoselectivity of benzylic hydroxylation catalysed by wild-type cytochrome P450BM3 using decoy molecules

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Abstract

The hydroxylation of non-native substrates catalysed by wild-type P450BM3 is reported, wherein “decoy molecules”, i.e., native substrate mimics, controlled the stereoselectivity of hydroxylation reactions. We employed decoy molecules with diverse structures, resulting in either a significant improvement in enantioselectivity or clear inversion of stereoselectivity in the benzylic hydroxylation of alkylbenzenes and cycloalkylbenzenes. For example, supplementation of wild-type P450BM3 with 5-cyclohexylvaleric acid-L-phenylalanine (5CHVA-Phe) and Z-proline-L-phenylalanine yielded 53% (R) ee and 56% (S) ee for indane hydroxylation, respectively, although 16% (S) ee was still observed in the absence of any additives. Moreover, we performed a successful crystal structure analysis of 5CHVA-L-tryptophan-bound P450BM3 at 2.00 Å, which suggests that the changes in selectivity observed were caused by conformational changes in the enzyme induced by binding of the decoy molecules.

Graphical abstract: Control of stereoselectivity of benzylic hydroxylation catalysed by wild-type cytochrome P450BM3 using decoy molecules

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Publication details

The article was received on 06 Jun 2017, accepted on 29 Jun 2017 and first published on 30 Jun 2017


Article type: Paper
DOI: 10.1039/C7CY01130J
Citation: Catal. Sci. Technol., 2017,7, 3332-3338
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    Control of stereoselectivity of benzylic hydroxylation catalysed by wild-type cytochrome P450BM3 using decoy molecules

    K. Suzuki, J. K. Stanfield, O. Shoji, S. Yanagisawa, H. Sugimoto, Y. Shiro and Y. Watanabe, Catal. Sci. Technol., 2017, 7, 3332
    DOI: 10.1039/C7CY01130J

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