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Enzyme‐Catalyzed Carbonyl Olefination by the E. coli Protein YfeX in the Absence of Phosphines
Author(s) -
Weissenborn Martin J.,
Löw Sebastian A.,
Borlinghaus Niels,
Kuhn Miriam,
Kummer Stefanie,
Rami Fabian,
Plietker Bernd,
Hauer Bernhard
Publication year - 2016
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201600227
Subject(s) - triphenylphosphine , wittig reaction , benzaldehyde , chemistry , catalysis , ethyl diazoacetate , triphenylarsine , enzyme , organic chemistry , medicinal chemistry , combinatorial chemistry , cyclopropanation
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.