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E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor

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E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor. / Summers, Benjamin D; Omar, Muhiadin; Ronson, Thomas O; Cartwright, Jared; Lloyd, Michael; Grogan, Gideon.

In: Organic & biomolecular chemistry, Vol. 13, 2015, p. 1897-1903.

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Harvard

Summers, BD, Omar, M, Ronson, TO, Cartwright, J, Lloyd, M & Grogan, G 2015, 'E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor', Organic & biomolecular chemistry, vol. 13, pp. 1897-1903. https://doi.org/10.1039/c4ob01441c

APA

Summers, B. D., Omar, M., Ronson, T. O., Cartwright, J., Lloyd, M., & Grogan, G. (2015). E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor. Organic & biomolecular chemistry, 13, 1897-1903. https://doi.org/10.1039/c4ob01441c

Vancouver

Summers BD, Omar M, Ronson TO, Cartwright J, Lloyd M, Grogan G. E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor. Organic & biomolecular chemistry. 2015;13:1897-1903. https://doi.org/10.1039/c4ob01441c

Author

Summers, Benjamin D ; Omar, Muhiadin ; Ronson, Thomas O ; Cartwright, Jared ; Lloyd, Michael ; Grogan, Gideon. / E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor. In: Organic & biomolecular chemistry. 2015 ; Vol. 13. pp. 1897-1903.

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@article{83e09c571486465b868aa0b524d4444f,
title = "E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor",
abstract = "The Baeyer-Villiger monooxygenase (BVMO) 'MO14' from Rhodococcus jostii RHA1, is an enantioselective BVMO that catalyses the resolution of the model ketone substrate bicyclo[3.2.0]hept-2-en-6-one to the (1S,5R)-2-oxa lactone and the residual (1S,5R)-substrate enantiomer. This regio-plus enantioselective behaviour is highly unusual for BVMOs, which often perform enantiodivergent biotransformations of this substrate. The scaleability of the transformation was investigated using fermentor-based experiments, in which variables including gene codon optimisation, temperature and substrate concentration were investigated. E. coli cells expressing MO14 catalysed the resolution of bicyclo[3.2.0]hept-2-en-6-one to yield (1S,5R)-2-oxa lactone of >99% ee and (1S,5R)-ketone of 96% ee after 14 h at a temperature of 16 °C and a substrate concentration of 0.5 g L(-1) (4.5 mM). MO14 is thus a promising biocatalyst for the production of enantio-enriched ketones and lactones derived from the [3.2.0] platform.",
author = "Summers, {Benjamin D} and Muhiadin Omar and Ronson, {Thomas O} and Jared Cartwright and Michael Lloyd and Gideon Grogan",
year = "2015",
doi = "10.1039/c4ob01441c",
language = "English",
volume = "13",
pages = "1897--1903",
journal = "Organic & biomolecular chemistry",
issn = "1477-0539",

}

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TY - JOUR

T1 - E. coli cells expressing the Baeyer-Villiger monooxygenase 'MO14' (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor

AU - Summers, Benjamin D

AU - Omar, Muhiadin

AU - Ronson, Thomas O

AU - Cartwright, Jared

AU - Lloyd, Michael

AU - Grogan, Gideon

PY - 2015

Y1 - 2015

N2 - The Baeyer-Villiger monooxygenase (BVMO) 'MO14' from Rhodococcus jostii RHA1, is an enantioselective BVMO that catalyses the resolution of the model ketone substrate bicyclo[3.2.0]hept-2-en-6-one to the (1S,5R)-2-oxa lactone and the residual (1S,5R)-substrate enantiomer. This regio-plus enantioselective behaviour is highly unusual for BVMOs, which often perform enantiodivergent biotransformations of this substrate. The scaleability of the transformation was investigated using fermentor-based experiments, in which variables including gene codon optimisation, temperature and substrate concentration were investigated. E. coli cells expressing MO14 catalysed the resolution of bicyclo[3.2.0]hept-2-en-6-one to yield (1S,5R)-2-oxa lactone of >99% ee and (1S,5R)-ketone of 96% ee after 14 h at a temperature of 16 °C and a substrate concentration of 0.5 g L(-1) (4.5 mM). MO14 is thus a promising biocatalyst for the production of enantio-enriched ketones and lactones derived from the [3.2.0] platform.

AB - The Baeyer-Villiger monooxygenase (BVMO) 'MO14' from Rhodococcus jostii RHA1, is an enantioselective BVMO that catalyses the resolution of the model ketone substrate bicyclo[3.2.0]hept-2-en-6-one to the (1S,5R)-2-oxa lactone and the residual (1S,5R)-substrate enantiomer. This regio-plus enantioselective behaviour is highly unusual for BVMOs, which often perform enantiodivergent biotransformations of this substrate. The scaleability of the transformation was investigated using fermentor-based experiments, in which variables including gene codon optimisation, temperature and substrate concentration were investigated. E. coli cells expressing MO14 catalysed the resolution of bicyclo[3.2.0]hept-2-en-6-one to yield (1S,5R)-2-oxa lactone of >99% ee and (1S,5R)-ketone of 96% ee after 14 h at a temperature of 16 °C and a substrate concentration of 0.5 g L(-1) (4.5 mM). MO14 is thus a promising biocatalyst for the production of enantio-enriched ketones and lactones derived from the [3.2.0] platform.

U2 - 10.1039/c4ob01441c

DO - 10.1039/c4ob01441c

M3 - Article

C2 - 25501564

VL - 13

SP - 1897

EP - 1903

JO - Organic & biomolecular chemistry

JF - Organic & biomolecular chemistry

SN - 1477-0539

ER -