Artificial Metalloenzymes through Cysteine-Selective Conjugation of Phosphines to Photoactive Yellow Protein

Pinning phosphines on proteins: A method for the cysteine‐selective bioconjugation of phosphines has been developed. The photoactive yellow protein has been site‐selectively functionalized with phosphine ligands and phosphine transition metal complexes to afford artificial metalloenzymes that are ac...

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Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2010-06, Vol.11 (9), p.1236-1239
Hauptverfasser:	Laan, Wouter, Muñoz, Bianca K, den Heeten, René, Kamer, Paul C.J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism bioconjugation Catalysis Cysteine - chemistry Halorhodospira halophila - metabolism hybrid catalysts metalloenzymes Palladium - chemistry Phosphines - chemistry Photoreceptors, Microbial - chemistry Photoreceptors, Microbial - genetics Photoreceptors, Microbial - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism transition metals
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Beschreibung
Zusammenfassung:	Pinning phosphines on proteins: A method for the cysteine‐selective bioconjugation of phosphines has been developed. The photoactive yellow protein has been site‐selectively functionalized with phosphine ligands and phosphine transition metal complexes to afford artificial metalloenzymes that are active in palladium‐catalysed allylic nucleophilic substitution reactions.
ISSN:	1439-4227 1439-7633
DOI:	10.1002/cbic.201000159