The C-terminal selenenylsulfide of extracellular/non-reduced thioredoxin reductase endows this protein with selectivity to small-molecule electrophilic reagents under oxidative conditions

The C-terminal selenenylsulfide of extracellular/non-reduced thioredoxin reductase endows this protein with selectivity to small-molecule electrophilic reagents under oxidative conditions

Mammalian cytosolic thioredoxin reductase (TrxR1) serves as an antioxidant protein by transferring electrons from NADPH to various substrates. The action of TrxR1 is achieved via reversible changes between NADPH-reduced and non-reduced forms, which involves C-terminal selenolthiol/selenenylsulfide e...

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Bibliographic Details
Main Authors: Huijun Qin, Chenchen Guo, Bozhen Chen, Hui Huang, Yaping Tian, Liangwei Zhong
Format: Article
Language:English
Published: Frontiers Media S.A. 2024-03-01
Series:Frontiers in Molecular Biosciences
Subjects:
thioredoxin reductase
selenocysteine
site-directed mutagenesis
protein complex
computer modeling
protein chemistry
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2024.1274850/full

Internet

https://www.frontiersin.org/articles/10.3389/fmolb.2024.1274850/full

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