Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymesCitation formats

  • External authors:
  • V. Köhler
  • Y. M. Wilson
  • M. Dürrenberger
  • D. Ghislieri
  • E. Churakova
  • T. Quinto
  • L. Knörr
  • D. Häussinger
  • F. Hollmann
  • T. R. Ward

Standard

Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes. / Köhler, V.; Wilson, Y. M.; Dürrenberger, M.; Ghislieri, D.; Churakova, E.; Quinto, T.; Knörr, L.; Häussinger, D.; Hollmann, F.; Turner, N. J.; Ward, T. R.

In: Nature Chemistry, Vol. 5, No. 2, 02.2013, p. 93-99.

Research output: Contribution to journalArticle

Harvard

Köhler, V, Wilson, YM, Dürrenberger, M, Ghislieri, D, Churakova, E, Quinto, T, Knörr, L, Häussinger, D, Hollmann, F, Turner, NJ & Ward, TR 2013, 'Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes' Nature Chemistry, vol. 5, no. 2, pp. 93-99. https://doi.org/10.1038/nchem.1498

APA

Köhler, V., Wilson, Y. M., Dürrenberger, M., Ghislieri, D., Churakova, E., Quinto, T., ... Ward, T. R. (2013). Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes. Nature Chemistry, 5(2), 93-99. https://doi.org/10.1038/nchem.1498

Vancouver

Köhler V, Wilson YM, Dürrenberger M, Ghislieri D, Churakova E, Quinto T et al. Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes. Nature Chemistry. 2013 Feb;5(2):93-99. https://doi.org/10.1038/nchem.1498

Author

Köhler, V. ; Wilson, Y. M. ; Dürrenberger, M. ; Ghislieri, D. ; Churakova, E. ; Quinto, T. ; Knörr, L. ; Häussinger, D. ; Hollmann, F. ; Turner, N. J. ; Ward, T. R. / Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes. In: Nature Chemistry. 2013 ; Vol. 5, No. 2. pp. 93-99.

Bibtex

@article{ad73417fa8724feabcf40195ed582c00,
title = "Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes",
abstract = "Enzymatic catalysis and homogeneous catalysis offer complementary means to address synthetic challenges, both in chemistry and in biology. Despite its attractiveness, the implementation of concurrent cascade reactions that combine an organometallic catalyst with an enzyme has proven challenging because of the mutual inactivation of both catalysts. To address this, we show that incorporation of a d 6 -piano stool complex within a host protein affords an artificial transfer hydrogenase (ATHase) that is fully compatible with and complementary to natural enzymes, thus enabling efficient concurrent tandem catalysis. To illustrate the generality of the approach, the ATHase was combined with various NADH-, FAD- and haem-dependent enzymes, resulting in orthogonal redox cascades. Up to three enzymes were integrated in the cascade and combined with the ATHase with a view to achieving (i) a double stereoselective amine deracemization, (ii) a horseradish peroxidase-coupled readout of the transfer hydrogenase activity towards its genetic optimization, (iii) the formation of L-pipecolic acid from L-lysine and (iv) regeneration of NADH to promote a monooxygenase-catalysed oxyfunctionalization reaction.{\circledC} 2013 Macmillan Publishers Limited. All rights reserved.",
author = "V. K{\"o}hler and Wilson, {Y. M.} and M. D{\"u}rrenberger and D. Ghislieri and E. Churakova and T. Quinto and L. Kn{\"o}rr and D. H{\"a}ussinger and F. Hollmann and Turner, {N. J.} and Ward, {T. R.}",
year = "2013",
month = "2",
doi = "10.1038/nchem.1498",
language = "English",
volume = "5",
pages = "93--99",
journal = "Nature Chemistry",
issn = "1755-4330",
publisher = "Springer Nature",
number = "2",

}

RIS

TY - JOUR

T1 - Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes

AU - Köhler, V.

AU - Wilson, Y. M.

AU - Dürrenberger, M.

AU - Ghislieri, D.

AU - Churakova, E.

AU - Quinto, T.

AU - Knörr, L.

AU - Häussinger, D.

AU - Hollmann, F.

AU - Turner, N. J.

AU - Ward, T. R.

PY - 2013/2

Y1 - 2013/2

N2 - Enzymatic catalysis and homogeneous catalysis offer complementary means to address synthetic challenges, both in chemistry and in biology. Despite its attractiveness, the implementation of concurrent cascade reactions that combine an organometallic catalyst with an enzyme has proven challenging because of the mutual inactivation of both catalysts. To address this, we show that incorporation of a d 6 -piano stool complex within a host protein affords an artificial transfer hydrogenase (ATHase) that is fully compatible with and complementary to natural enzymes, thus enabling efficient concurrent tandem catalysis. To illustrate the generality of the approach, the ATHase was combined with various NADH-, FAD- and haem-dependent enzymes, resulting in orthogonal redox cascades. Up to three enzymes were integrated in the cascade and combined with the ATHase with a view to achieving (i) a double stereoselective amine deracemization, (ii) a horseradish peroxidase-coupled readout of the transfer hydrogenase activity towards its genetic optimization, (iii) the formation of L-pipecolic acid from L-lysine and (iv) regeneration of NADH to promote a monooxygenase-catalysed oxyfunctionalization reaction.© 2013 Macmillan Publishers Limited. All rights reserved.

AB - Enzymatic catalysis and homogeneous catalysis offer complementary means to address synthetic challenges, both in chemistry and in biology. Despite its attractiveness, the implementation of concurrent cascade reactions that combine an organometallic catalyst with an enzyme has proven challenging because of the mutual inactivation of both catalysts. To address this, we show that incorporation of a d 6 -piano stool complex within a host protein affords an artificial transfer hydrogenase (ATHase) that is fully compatible with and complementary to natural enzymes, thus enabling efficient concurrent tandem catalysis. To illustrate the generality of the approach, the ATHase was combined with various NADH-, FAD- and haem-dependent enzymes, resulting in orthogonal redox cascades. Up to three enzymes were integrated in the cascade and combined with the ATHase with a view to achieving (i) a double stereoselective amine deracemization, (ii) a horseradish peroxidase-coupled readout of the transfer hydrogenase activity towards its genetic optimization, (iii) the formation of L-pipecolic acid from L-lysine and (iv) regeneration of NADH to promote a monooxygenase-catalysed oxyfunctionalization reaction.© 2013 Macmillan Publishers Limited. All rights reserved.

U2 - 10.1038/nchem.1498

DO - 10.1038/nchem.1498

M3 - Article

VL - 5

SP - 93

EP - 99

JO - Nature Chemistry

JF - Nature Chemistry

SN - 1755-4330

IS - 2

ER -