1246636-34-9Relevant academic research and scientific papers
Highly efficient and site-selective phosphane modification of proteins through hydrazone linkage: Development of artificial metalloenzymes
Deuss, Peter J.,Popa, Gina,Botting, Catherine H.,Laan, Wouter,Kamer, Paul C. J.
supporting information; experimental part, p. 5315 - 5317 (2010/10/20)
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.
