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Inside Cover: Caged Glutathione – Triggering Protein Interaction by Light (Angew. Chem. Int. Ed. 16/2012)
Author(s) -
Gatterdam Volker,
Stoess Tatjana,
Menge Clara,
Heckel Alexander,
Tampé Robert
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201327
Subject(s) - glutathione , chemistry , scavenger , reactive oxygen species , substrate (aquarium) , int , redox , cover (algebra) , biophysics , antioxidant , biochemistry , enzyme , biology , organic chemistry , ecology , mechanical engineering , computer science , engineering , operating system
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.