Highly Efficient and Site-Selective Phosphane Modification of Proteins through Hydrazone Linkage: Development of Artificial Metalloenzymes

Authors


  • 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.

Abstract

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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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