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Directed Evolution of Artificial Metalloenzymes

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons137019

Ilie,  Adriana
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Philipps-Universität Marburg, Fachbereich Chemie;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons58919

Reetz,  Manfred T.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Philipps-Universität Marburg, Fachbereich Chemie;

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Citation

Ilie, A., & Reetz, M. T. (2015). Directed Evolution of Artificial Metalloenzymes. Israel Journal of Chemistry, 55, 51-60. doi:10.1002/ijch.201400087.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-561D-9
Abstract
Transition metal catalysis in asymmetric transformations plays a pivotal role in modern synthetic organic chemistry, with these catalysts being tuned by systematic variation of the chiral ligand. More than three decades ago it was recognized that an alternative approach is possible, namely the anchoring of an achiral ligand/metal entity in an appropriate protein host, with formation of an artificial metalloenzyme (hybrid catalyst). However, this procedure delivers a single transition metal catalyst, with high enantioselectivity being a matter of chance. In view of this restriction, we proposed in 2001/2002 the concept of directed evolution of such hybrid catalysts. The most intensively studied system involves biotinylated phosphine/metal entities which are non-covalently anchored to streptavidin. The present review summarizes progress in this intriguing area of research. It includes the assessment of the requirements of a given Darwinian system to be successful, and offers hints on how to achieve success in future studies.