Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-02

AUTHORS

V. Köhler, Y. M. Wilson, M. Dürrenberger, D. Ghislieri, E. Churakova, T. Quinto, L. Knörr, D. Häussinger, F. Hollmann, N. J. Turner, T. R. Ward

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. More... »

PAGES

93

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchem.1498

DOI

http://dx.doi.org/10.1038/nchem.1498

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1033564902

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23344429


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