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Guiding bar motif of thioredoxin reductase 1 modulates enzymatic activity and inhibitor binding by communicating with the co-factor FAD and regulating the flexible C-terminal redox motif

Redox biology. 2024-01; 
Wuyang Shi , Shibo Sun , Haowen Liu , Yao Meng , Kangshuai Ren , Guoying Wang , Minghui Liu , Jiaqi Wu , Yue Zhang , Huang Huang , Meiyun Shi , Weiping Xu , Qiang Ma , Bingbing Sun , Jianqiang Xu
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摘要

Thioredoxin reductase (TXNRD) is a selenoprotein that plays a crucial role in cellular antioxidant defense. Previously, a distinctive guiding bar motif was identified in TXNRD1, which influences the transfer of electrons. In this study, utilizing single amino acid substitution and Excitation-Emission Matrix (EEM) fluorescence spectrum analysis, we discovered that the guiding bar communicates with the FAD and modulates the electron flow of the enzyme. Differential Scanning Fluorimetry (DSF) analysis demonstrated that the aromatic amino acid in guiding bar is a stabilizer for TXNRD1. Kinetic analysis revealed that the guiding bar is vital for the disulfide reductase activity but hinders the selenocyste... More

關鍵詞

Thioredoxin reductase Thioredoxin Selenoprotein Guiding bar motif Caveolin-1 LCS3
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