Journal
NATURE CHEMISTRY
Volume 5, Issue 2, Pages 93-99Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.1498
Keywords
-
Categories
Funding
- Marie Curie Initial Training Network [FP7 ITN 238531]
- SNF (Schweizerische Nationalfonds) [200020_126366]
- National Centre of Competence in Research Nanosciences
- Royal Society
- Swiss National Science Foundation (SNF) [200020_126366] Funding Source: Swiss National Science Foundation (SNF)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available