A Diselenide turn-on Fluorescent Probe for the Detection of Thioredoxin Reductase.

@article{Mafireyi2020ADT,
  title={A Diselenide turn-on Fluorescent Probe for the Detection of Thioredoxin Reductase.},
  author={Tendai Mafireyi and Madeleine Laws and John W. Bassett and Pamela B. Cassidy and Jorge O. Escobedo and Robert M. Strongin},
  journal={Angewandte Chemie},
  year={2020},
  url={https://api.semanticscholar.org/CorpusID:218873258}
}
The first diselenide-based probe for the selective detection of thioredoxin reductase (TrxR), an enzyme commonly overexpressed in melanomas, is reported, showing improved signaling of TrxR activity compared to the disulfide analogue.

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Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells.

The first fluorescent probe for mammalian thioredoxin reductase (TrxR), TRFS-green, was designed, synthesized, and fully evaluated and is expected to facilitate the discovery of TrxR-targeting small molecules for potential therapeutic agents and provide significant advances in understanding the physiological/pathophysiological functions of TrXR in vivo.

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A model for the interaction between TrxR and dinitrohalobenzenes is proposed, involving a functional FAD in the alkylated TrXR generating an anion nitroradical in a dinitrophenyl group, which in turn reacts with oxygen to generate superoxide.

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Thioredoxin reductase.

The importance of Trx to many aspects of cell function make it likely that TrxRs also play a role in protection against oxidant injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form.