Cover Feature: Highly Electrophilic Intermediates in the Bypass Mechanism of Glutathione Peroxidase: Synthesis, Reactivity, and Structures of Selenocysteine‐Derived Cyclic Selenenyl Amides (Chem. Eur. J. 71/2023)

The cover picture shows key players in the catalytic cycle of the mammalian antioxidant enzyme, glutathione peroxidase (GPx). Selenocysteine selenenic acids (queen) and selenocysteine selenenyl sulfides (rook) are established contributors to GPx function. This study unveils a previously overlooked c...

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Bibliographic Details
Published in:Chemistry : a European journal 2023-12, Vol.29 (71), p.n/a
Main Authors: Masuda, Ryosuke, Karasaki, Takafumi, Sase, Shohei, Kuwano, Satoru, Goto, Kei
Format: Article
Language:English
Subjects:
Amides
Chemistry
Chess
cyclic selenenyl amides
Glutathione
Glutathione peroxidase
glutathione peroxidases
Inactivation
Intermediates
molecular cradles
Peroxidase
Selenocysteine
selenocysteines
selenoproteins
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Summary:The cover picture shows key players in the catalytic cycle of the mammalian antioxidant enzyme, glutathione peroxidase (GPx). Selenocysteine selenenic acids (queen) and selenocysteine selenenyl sulfides (rook) are established contributors to GPx function. This study unveils a previously overlooked class of intermediates: selenocysteine cyclic selenenyl amides (king). Through model studies, their reactivity has been revealed, exhibiting dual functionality. They not only prevent the inactivation of GPx but also act as highly electrophilic intermediates in selenoprotein reactions. Their roles mirror a chess king, dynamically adapting to their application. More information can be found in the Research Article by K. Goto et al. (DOI: 10.1002/chem.202302615).
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.202303729