Fluorescence-Based Assay for the Optimization of the Activity of Artificial Transfer Hydrogenase within a Biocompatible Compartment

  • Heinisch T
  • Langowska K
  • Tanner P
 et al. 
  • 28


    Mendeley users who have this article in their library.
  • 19


    Citations of this article.


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.

Author-supplied keywords

  • Enones
  • Fluorescence
  • Hydrogenation
  • Metalloenzymes
  • Nanostructures

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Tillmann Heinisch

  • Karolina Langowska

  • Pascal Tanner

  • Jean Louis Reymond

  • Wolfgang Meier

  • Cornelia Palivan

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free