The IPB has once again been recognized for its exemplary actions in terms of equal opportunity-oriented personnel and organizational policies and has received the TOTAL E-QUALITY certification for the…
The Plant Science Student Conference (PSSC) has been organised by students from the two Leibniz institutes, IPK and IPB, every year for the last 20 years. In this interview, Christina Wäsch (IPK) and…
Weissenborn, M. J.; Löw, S. A.; Borlinghaus, N.; Kuhn, M.; Kummer, S.; Rami, F.; Plietker, B.; Hauer, B.;Enzyme-Catalyzed Carbonyl Olefination by the E. coli Protein YfeX in the Absence of PhosphinesChemCatChem81636-1640(2016)DOI: 10.1002/cctc.201600227
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.