We thank the European Union (Marie Curie excellence grant MEXT-2004-014320); NEST Adventure STREP Project artizymes (contract no. FP6-2003-NEST-B3 15471); Network of Excellence Idecat (Idecat-CT-2005-011730); COST action (CM0802 PhoSciNet), EASTCHEM, and Sasol for funding. We also thank Dr. T. Glumoff (University of Oulu, Finland) and Prof. Dr. K. J. Hellingwerf (University of Amsterdam) for providing plasmids and the Wellcome Trust for funding the purchase of the instruments.
Highly Efficient and Site-Selective Phosphane Modification of Proteins through Hydrazone Linkage: Development of Artificial Metalloenzymes†
Article first published online: 22 JUN 2010
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 31, pages 5315–5317, July 19, 2010
How to Cite
Deuss, Peter J., Popa, G., Botting, Catherine H., Laan, W. and Kamer, Paul C. J. (2010), Highly Efficient and Site-Selective Phosphane Modification of Proteins through Hydrazone Linkage: Development of Artificial Metalloenzymes. Angew. Chem. Int. Ed., 49: 5315–5317. doi: 10.1002/anie.201002174
- Issue published online: 16 JUL 2010
- Article first published online: 22 JUN 2010
- Manuscript Received: 13 APR 2010
- European Union
- MEXT. Grant Number: 2004-014320
- NEST Adventure STREP. Grant Number: FP6-2003-NEST-B3 15471
- Network of Excellence Idecat. Grant Number: Idecat-CT-2005-011730
A joint effort: A novel, highly efficient, and selective procedure for phosphane modification of proteins is reported (see scheme). This method involves cysteine modification with a maleimide containing a hydrazide functional group and subsequent hydrazone formation with phosphane aldehydes. Mono- and bidentate phosphane ligands were successfully coupled to several proteins, one of which was coordinated to rhodium to give an artificial metalloenzyme.