Enzyme‐Catalyzed Carbonyl Olefination by the <i>E. coli</i> Protein YfeX in the Absence of Phosphines

Martin J. Weissenborn, Sebastian A. Löw, Niels Borlinghaus, Miriam Kuhn, Stefanie Kummer, Fabian Rami, Bernd Plietker, Bernhard Hauer

ChemCatChem · 2016 · 54 citations · 27 references

Concepts

Abstract

Abstract The Wittig‐type carbonyl olefination reaction has no biocatalytic equivalent. To build complex molecular scaffolds, however, C−C bond‐forming reactions are pivotal for biobased economy and synthetic biology. The heme‐containing E. coli protein YfeX was found to catalyze carbonyl olefination by reaction of benzaldehyde with ethyl diazoacetate under aerobic conditions in the absence of a triphenylphosphine oxophile. The reaction was performed in whole cells and showed a product formation of 440 mg L −1 in 1 h. It was, moreover, shown that the reaction could be performed under Wittig‐analogue conditions in the presence of triphenylphosphine or triphenylarsine.

References

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