Enantioselective Organometallic Enzyme Hybrid (OMEH) Catalysts

  • Author: Saskia Neubacher
  • Published Date: 21 June 2013
  • Source / Publisher: ChemistryOpen/Wiley-VCH
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA
thumbnail image: Enantioselective Organometallic Enzyme Hybrid (OMEH) Catalysts

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Artificial metalloenzymes could greatly expand the range of reactions accessible by biocatalysis. So far, the most successful strategy to achieve good catalytic activities and enantioselectivities has been through site-directed anchoring of artificial cofactors representing appropriate ligands or metal complexes.

Jörg Eppinger and co-workers, King Abdullah University of Science and Technology, Saudi Arabia, designed modular metal-conjugated affinity labels. They consist of three units:

  1. an achiral, catalytically active metal complex,
  2. a protease-specific reactive group that is able to form a covalent bond with the active center of the enzyme, and
  3. a peptidic affinity tail to direct the binding orientation.

They show that variation of the metal center, affinity tail, and the host protein influence the enantioselectivities of a ketone hydrogenation and achieve enantiomeric ratios of up to 82:18.

The modular setup enables a rapid generation of artificial metalloenzyme libraries, which can be adapted to a broad range of catalytic conditions.

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