Inhibition and crosslinking of the selenoprotein thioredoxin reductase-1 by p-benzoquinone

@inproceedings{Shu2019InhibitionAC,
  title={Inhibition and crosslinking of the selenoprotein thioredoxin reductase-1 by p-benzoquinone},
  author={N. C. Shu and Qing Cheng and Elias S J Arn{\'e}r and Michael J Davies},
  booktitle={Redox biology},
  year={2019}
}
Quinones are common in nature, and often cytotoxic. Their proposed toxicity mechanisms involve redox cycling with radical generation, and/or reactions with nucleophiles, such as protein cysteine (Cys) residues, forming adducts via Michael addition reactions. The selenenyl anion of selenocysteine (Sec) is a stronger nucleophile, more prevalent at physiological pH, and more reactive than the corresponding thiolate anion of Cys. We therefore hypothesized that Sec residues should be readily… CONTINUE READING

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