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Enzyme Activity by Design: An Artificial Rhodium Hydroformylase for Linear Aldehydes
Author(s) -
Jarvis Amanda G.,
Obrecht Lorenz,
Deuss Peter J.,
Laan Wouter,
Gibson Emma K.,
Wells Peter P.,
Kamer Paul C. J.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201705753
Subject(s) - bioconjugation , chemistry , reactivity (psychology) , rhodium , catalysis , phosphine , combinatorial chemistry , natural product , selectivity , artificial enzyme , organic chemistry , medicine , alternative medicine , pathology
Artificial metalloenzymes (ArMs) are hybrid catalysts that offer a unique opportunity to combine the superior performance of natural protein structures with the unnatural reactivity of transition‐metal catalytic centers. Therefore, they provide the prospect of highly selective and active catalytic chemical conversions for which natural enzymes are unavailable. Herein, we show how by rationally combining robust site‐specific phosphine bioconjugation methods and a lipid‐binding protein (SCP‐2L), an artificial rhodium hydroformylase was developed that displays remarkable activities and selectivities for the biphasic production of long‐chain linear aldehydes under benign aqueous conditions. Overall, this study demonstrates that judiciously chosen protein‐binding scaffolds can be adapted to obtain metalloenzymes that provide the reactivity of the introduced metal center combined with specifically intended product selectivity.