Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes

New Cover Article in ChemistryOPEN

4/23/2013

The cover picture illustrates the concept of using metal-conjugated affinity labels (m-ALs) to convert proteases into well-defined and catalytically active artificial metalloenzymes. The X-ray structure of the papain-bound inhibitor E64c (orange) served as the basis to predict the orientation of the half-sandwich rhodium(III) moiety (yellow sphere) within the binding pocket of the protease. The well-defined position of the affinity label on the protein surface leads to a distinct environment of the metal center, which translates into enantiomeric ratios of up to 82:18 in the aqueous hydrogenation of ketones.


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How to train a protein: Metal-conjugated affinity labels were used to selectively position catalytically active metal centers in the binding pocket of proteases. The resulting artificial metalloenzymes achieve up to 82 % e.r. in the hydrogenation of ketones. The modular setup enables a rapid generation of artificial metalloenzyme libraries, which can be adapted to a broad range of catalytic conditions.

For more details, see the Communication: