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Peter J. Deuss, Gina Popa, Catherine H. Botting, Wouter Laan and Paul C. J. Kamer Highly Efficient and Site-Selective Phosphane Modification of Proteins through Hydrazone Linkage: Development of Artificial Metalloenzymes Angewandte Chemie International Edition 49

Version of Record online: 22 JUN 2010 | DOI: 10.1002/anie.201002174

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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.

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