Journalartikel

Jahr der Veröffentlichung: 2003

Seiten: 2848-2852

Zeitschrift: Organic & Biomolecular Chemistry

Bandnummer: 1

Heftnummer: 16

ISSN: 1477-0520

eISSN: 1477-0539

DOI Link: https://doi.org/10.1039/b302220j

Verlag: Royal Society of Chemistry

Abstract: 
Areneselenenyl iodide stabilised by internal chelation has been synthesized and evaluated as a substrate of thioredoxin reductase (TrxR). The reactivity of TrxR obtained from human placenta towards selenenyl iodide was found to be much higher than that of the E coli enzyme, indicating the essential nature of a selenocysteine residue in the active site of the human enzyme. The addition of thioredoxin (Trx) significantly enhanced the TrxR-catalysed reduction of selenenyl iodide 1. These studies on the reduction of a selenenyl iodide by the thioredoxin system suggest that stable selenenyl iodides could be new substrates for human TrxR. The Trx system could act as a cofactor for iodothyronine deiodinase by reducing the selenenyl iodide intermediate in the second-half of the deiodinase catalytic cycle to regenerate the active site. The TrxR-catalysed reduction of 1 was not inhibited by the anti-thyroid drug, PTU, suggesting that the involvement of the Trx system in the deiodinase cycle may be responsible for the insensitivity of certain deiodinases towards clinically useful thiourea drugs.

Harvard-Zitierstil: Mugesh, G., Klotz, L., du Mont, W., Becker, K. and Sies, H. (2003) Selenenyl iodide: a new substrate for mammalian thioredoxin reductase, Organic and Biomolecular Chemistry, 1(16), pp. 2848-2852. https://doi.org/10.1039/b302220j

APA-Zitierstil: Mugesh, G., Klotz, L., du Mont, W., Becker, K., & Sies, H. (2003). Selenenyl iodide: a new substrate for mammalian thioredoxin reductase. Organic and Biomolecular Chemistry. 1(16), 2848-2852. https://doi.org/10.1039/b302220j