Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)

Thomas Reiner,Alexander N Marziale,Dominik Jantke,Jörg Eppinger,Andreas Raba

doi:10.1002/open.201390005

Thomas Reiner, Alexander N Marziale + Show 3 more

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https://doi.org/10.1002/open.201390005

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Abstract

Cover PictureThomas Reiner, Dominik Jantke, Alexander N. Marziale, Andreas Raba, and Jörg Eppinger*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. For more details, see the Communication by Jörg Eppinger et al., on p. 50 ff.

Highlights

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 served as the basis to predict the orientation of the half-sandwich rhodium(III) moiety 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

Summary

Introduction

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.

Results

Conclusion