Efficient in situ regeneration of NADH mimics by an artificial metalloenzyme

Yasunori Okamoto, Valentin Köhler, Caroline E. Paul, Frank Hollmann, Thomas R. Ward

Research output: Contribution to journalArticlepeer-review

89 Citations (Scopus)


NADH mimics (mNADHs) have been shown to accelerate and orthogonally activate ene reductase-catalyzed reactions. However, existing regeneration methods of NAD(P)H fail for mNADHs. Catalysis with artificial metalloenzymes based on streptavidin (Sav) variants and a biotinylated iridium cofactor enable mNADH regeneration with formate. This regeneration can be coupled with ene reductase-catalyzed asymmetric reduction of α,β-unsaturated compounds, because of the protective compartmentalization of the organometallic cofactor. With 10 mol% mNAD+, a preparative scale reaction (>100 mg) gave full conversion with 98% ee, where TTNs reached 2000, with respect to the Ir cofactor under ambient atmosphere in aqueous medium.

Original languageEnglish
Pages (from-to)3553-3557
Number of pages5
JournalACS Catalysis
Issue number6
Publication statusPublished - 2016 Jun 3


  • artificial metalloenzyme
  • asymmetric catalysis
  • biocatalysis
  • iridium
  • renewable source


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