Inside Cover

Inside Cover: Caged Glutathione – Triggering Protein Interaction by Light (Angew. Chem. Int. Ed. 16/2012)

  1. Volker Gatterdam1,†,
  2. Tatjana Stoess2,†,
  3. Clara Menge2,
  4. Prof. Dr. Alexander Heckel2,*,
  5. Prof. Dr. Robert Tampé1,*

Article first published online: 8 MAR 2012

DOI: 10.1002/anie.201201327

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 51, Issue 16, page 3726, April 16, 2012

Additional Information

How to Cite

Gatterdam, V., Stoess, T., Menge, C., Heckel, A. and Tampé, R. (2012), Inside Cover: Caged Glutathione – Triggering Protein Interaction by Light (Angew. Chem. Int. Ed. 16/2012). Angew. Chem. Int. Ed., 51: 3726. doi: 10.1002/anie.201201327

Author Information

  1. 1

    Institute of Biochemistry, Biocenter, Cluster of Excellence Frankfurt (CEF), Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438 Frankfurt am Main (Germany) http://www.biochem.uni-frankfurt.de

  2. 2

    Frankfurt Institute for Molecular Life Sciences, Cluster of Excellence Frankfurt (CEF), Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438 Frankfurt am Main (Germany)

  1. †

    Both authors contributed equally to this work.

*Frankfurt Institute for Molecular Life Sciences, Cluster of Excellence Frankfurt (CEF), Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438 Frankfurt am Main (Germany)

  1. †

    Both authors contributed equally to this work.

Publication History

  1. Issue published online: 11 APR 2012
  2. Article first published online: 8 MAR 2012

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Keywords:

  • glutathione S-transferase;
  • light-triggered chemical biology;
  • photoactivatable compounds;
  • photoactivation;
  • protein immobilization
Thumbnail image of graphical abstract

Caged glutathione is a new way to trigger protein interaction by light. Glutathione fulfills a universal role as redox factor, scavenger of reactive oxygen species, and as an essential substrate in the conjugation, detoxification, and reduction reactions catalyzed by glutathione S-transferase (GST). In their Communication on page 3960 ff., A. Heckel, R. Tampé and co-workers describe how GST fusion proteins could be assembled in situ at variable density by laser-scanning activation.

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