Advanced Synthesis & Catalysis
Copyright © 2015 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
Editor: Joe P. Richmond, Chairman of the Editorial Board: Ryoji Noyori
Impact Factor: 5.542
ISI Journal Citation Reports © Ranking: 2013: 2/71 (Chemistry Applied); 5/58 (Chemistry Organic)
Online ISSN: 1615-4169
Associated Title(s): Angewandte Chemie International Edition, Asian Journal of Organic Chemistry, Chemistry - A European Journal, Chemistry – An Asian Journal, ChemCatChem, European Journal of Organic Chemistry
Cover Picture: Biocatalytic Imine Reduction and Reductive Amination of Ketones (Adv. Synth. Catal. 8/2015)
Biocatalytic imine reduction: Recent years have seen impressive progress in the biocatalytic asymmetric reduction of imines and reductive amination of ketones. Several new classes of enzymes have been introduced for these reactions, such as amine dehydrogenases, imine reductases, and artificial transfer hydrogenases. The front cover picture shows a selection of products accessible via biocatalytic C=N reduction – including amino acid conjugates and natural alkaloids – along with a reductive-amination biocatalyst, an opine dehydrogenase (artwork designed by Verena A. Resch). Details can be found in the review on pages 1655–1685 (J. H. Schrittwieser, S. Velikogne, W. Kroutil, Adv. Synth. Catal. 2015, 357, 1655–1685; DOI: 10.1002/adsc.201500213).
Inside Cover: Artificial Metalloenzymes in Asymmetric Catalysis: Key Developments and Future Directions (Adv. Synth. Catal. 8/2015)
The inside cover picture by Oscar Pàmies, Montserrat Diéguez and Jan-E. Bäckvall illustrates the formation of an artificial metalloenzyme as two puzzle pieces that fit perfectly. One piece is an enzyme. The other is a metallic fragment. This review discusses all the developed strategies and the latest advances in the synthesis and application in asymmetric catalysis of artificial metalloenzymes with future directions for their design, synthesis and application. Advice is also presented (for the non-specialist) how to prepare and use artificial metalloenzymes. Details can be found in the review on pages 1567–1586 (O. Pàmies, M. Diéguez, J.-E. Bäckvall, Adv. Synth. Catal. 2015, 357, 1567–1586; DOI: 10.1002/adsc.201500290).
Inside Back Cover: Complete Enzymatic Oxidation of Methanol to Carbon Dioxide: Towards More Eco-Efficient Regeneration Systems for Reduced Nicotinamide Cofactors (Adv. Synth. Catal. 8/2015)
The inside back cover picture, provided by Selin Kara et al., illustrates an in situ NADH regeneration cascade comprising alcohol dehydrogenase, formaldehyde dismutase and formate dehydrogenase. This system principally enables complete oxidation of methanol to CO2 thereby yielding 3 equivalents on NADH per mole of methanol employed, thereby representing a very atom efficient regeneration system (artwork designed by Verena A. Resch). Details can be found in the communication on pages 1687–1691 (S. Kara, J. H. Schrittwieser, S. Gargiulo, Y. Ni, H. Yanase, D. J. Opperman, W. J. H. van Berkel, F. Hollmann, Adv. Synth. Catal. 2015, 357, 1687–1691; DOI: 10.1002/adsc.201500173).