SEARCH

SEARCH BY CITATION

Keywords:

  • affinity labels;
  • artificial metalloproteins;
  • asymmetric catalysis;
  • cysteine proteases;
  • hydrogenation
Thumbnail image of graphical abstract

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.