Communication

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

  1. Wouter Laan Dr.1,
  2. Bianca K. Muñoz Dr.1,
  3. René den Heeten Dr.2,
  4. Paul C. J. Kamer Prof. Dr.1

Article first published online: 29 APR 2010

DOI: 10.1002/cbic.201000159

Issue

ChemBioChem

ChemBioChem

Volume 11, Issue 9, pages 1236–1239, June 14, 2010

Additional Information

How to Cite

Laan, W., Muñoz, B. K., den Heeten, R. and Kamer, P. C. J. (2010), Artificial Metalloenzymes through Cysteine-Selective Conjugation of Phosphines to Photoactive Yellow Protein. ChemBioChem, 11: 1236–1239. doi: 10.1002/cbic.201000159

Author Information

  1. 1

    School of Chemistry, University of St Andrews, North Haugh, KY16 9ST, St. Andrews (UK), Fax: (+44) 1334463808

  2. 2

    Van 't Hoff Institute for Molecular Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam (NL)

Publication History

  1. Issue published online: 7 JUN 2010
  2. Article first published online: 29 APR 2010
  3. Manuscript Received: 10 MAR 2010

Funded by

  • NRSCC
  • European Union. Grant Number: FP6-2003-NEST-B3 15471
  • Marie Curie Excellence Grants. Grant Number: MEXT-2004-014320

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Keywords:

  • bioconjugation;
  • catalysis;
  • hybrid catalysts;
  • metalloenzymes;
  • transition metals
Thumbnail image of graphical abstract

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.

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