Journal
ACS CATALYSIS
Volume 6, Issue 6, Pages 3553-3557Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.6b00258
Keywords
artificial metalloenzyme; iridium; biocatalysis; renewable source; asymmetric catalysis
Categories
Funding
- Swiss National Science Foundation [200020_162348]
- NCCR Molecular Systems Engineering
- Swiss National Science Foundation (SNF) [200020_162348] Funding Source: Swiss National Science Foundation (SNF)
Ask authors/readers for more resources
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 (Say) variants and a biotinylated iridium cofactor enable mNADH regeneration with formate. This regeneration can be coupled with ene reductase-catalyzed asymmetric reduction of a,fi-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.
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