These authors contributed equally to this work.
X-Ray Structure and Designed Evolution of an Artificial Transfer Hydrogenase†
Article first published online: 4 JAN 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 47, Issue 8, pages 1400–1404, February 8, 2008
How to Cite
Creus, M., Pordea, A., Rossel, T., Sardo, A., Letondor, C., Ivanova, A., LeTrong, I., Stenkamp, Ronald E. and Ward, Thomas R. (2008), X-Ray Structure and Designed Evolution of an Artificial Transfer Hydrogenase. Angew. Chem. Int. Ed., 47: 1400–1404. doi: 10.1002/anie.200704865
This work was funded by the Swiss National Science Foundation (Grants FN 200021-105192 and 200020-113348), the Roche Foundation as well as the FP6 Marie Curie Research Training network (MRTN-CT-2003-505020) and the Canton of Neuchâtel. We thank Umicore Precious Metals Chemistry for a loan of ruthenium. We thank C. R. Cantor for the streptavidin gene.
- Issue published online: 4 FEB 2008
- Article first published online: 4 JAN 2008
- Manuscript Received: 19 OCT 2007
- Swiss National Science Foundation. Grant Numbers: 200021-105192, 200020-113348
- Roche Foundation
- FP6 Marie Curie Research Training network. Grant Number: MRTN-CT-2003-505020
- Canton of Neuchâtel
- asymmetric catalysis;
- chemogenetic optimization;
- directed evolution;
A structure is worth a thousand words: Guided by the X-ray structure of an S-selective artificial transfer hydrogenase, designed evolution was used to optimize the selectivity of hybrid catalysts. Fine-tuning of the second coordination sphere of the ruthenium center (see picture, orange sphere) by introduction of two point mutations allowed the identification of selective artificial transfer hydrogenases for the reduction of dialkyl ketones.