Front Cover: S‐Denitrosylase‐Like Activity of Cyclic Diselenides Conjugated with Xaa‐His Dipeptide: Role of Proline Spacer as a Key Activity Booster (ChemBioChem 5/2022)

Diselenide‐based S‐denitrosylase mimic: This study demonstrates the potential of 1,2‐diselenan‐4‐amine conjugated with Pro‐His dipeptide as a novel S‐denitrosylase mimic, which catalytically promotes cysteinyl S‐denitrosylation in the presence of a thiol co‐substrate and prevents protein misfolding...

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Veröffentlicht in:Chembiochem : a European journal of chemical biology 2022-03, Vol.23 (5), p.n/a
Hauptverfasser: Mikami, Rumi, Tsukagoshi, Shunsuke, Oda, Yoshiki, Arai, Kenta
Format: Artikel
Sprache:eng
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Zusammenfassung:Diselenide‐based S‐denitrosylase mimic: This study demonstrates the potential of 1,2‐diselenan‐4‐amine conjugated with Pro‐His dipeptide as a novel S‐denitrosylase mimic, which catalytically promotes cysteinyl S‐denitrosylation in the presence of a thiol co‐substrate and prevents protein misfolding caused by S‐nitrosylation. The cover image shows how the catalytic cycle involved a highly reactive diselenol species forming a γ‐turn structure, and highlights the mystique of the reaction controlled by Selene, goddess of the moon and origin of the name for the element, selenium. More information can be found in the Full Paper by K. Arai et al.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.202100558