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Caged Glutathione – Triggering Protein Interaction by Light
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 - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201108073
Subject(s) - glutathione , scavenger , reactive oxygen species , substrate (aquarium) , glutathione s transferase , chemistry , redox , detoxification (alternative medicine) , biochemistry , antioxidant , enzyme , biology , organic chemistry , medicine , ecology , alternative medicine , pathology
Light, GSH, action! Glutathione (GSH) 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). A photoactivatable glutathione allows the GSH‐GST network to be triggered by light. GST fusion proteins can be assembled in situ at variable density and structures by laser‐scanning activation.