Back Cover: Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology (ChemCatChem 4/2014). Issue 4 (April 2014)

• Record Type: Journal Article
• Authors: Quinto, Tommaso; Schwizer, Fabian; Zimbron, Jeremy M.; Morina, Albert; Köhler, Valentin; Ward, Thomas R.
• Is Part Of: ChemCatChem. Volume 6:Issue 4(2014:Apr.)
• Page Start: 1120
• Page End: 1120
• Publication Date: 2014-04
• Subjects: Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201490026
• Languages: English
• ISSNs: 1867-3880

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Powerful diversification</bold> The cover picture presents a novel strategy for rapid access to chemogenetic diversity for artificial transfer hydrogenases (ATHases) based on the biotin–streptavidin technology. In their Full Paper on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 1010 ff.</ext-link>, T. R. Ward et al. outline a straightforward optimization approach whereby a biotinylated pentamethylcyclopentadienyl iridium is combined with a library of bidentate ligands in the presence of streptavidin variants. The performance of the resulting ATHase is evaluated for the enantioselective reduction of cyclic imines, leading to the identification of α‐amino amides as the most versatile ligands.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg58fdr2vz" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>