Efficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme

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...

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Bibliographic Details
Published inACS catalysis Vol. 6; no. 6; pp. 3553 - 3557
Main Authors Okamoto, Yasunori, Köhler, Valentin, Paul, Caroline E, Hollmann, Frank, Ward, Thomas R
Format Journal Article
LanguageEnglish
Published American Chemical Society 03.06.2016
Subjects
iridium
artificial metalloenzyme
asymmetric catalysis
biocatalysis
renewable source
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Summary: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.
ISSN:2155-5435
2155-5435
DOI:10.1021/acscatal.6b00258