Reduction of Tetrathionate by Mammalian Thioredoxin Reductase

Vivek Narayan, Avinash K. Kudva, K. Sandeep Prabhu

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Tetrathionate, a polythionate oxidation product of microbial hydrogen sulfide and reactive oxygen species from immune cells in the gut, serves as a terminal electron acceptor to confer a growth advantage for Salmonella and other enterobacteria. Here we show that the rat liver selenoenzyme thioredoxin reductase (Txnrd1, TR1) efficiently reduces tetrathionate in vitro. Furthermore, lysates of selenium-supplemented murine macrophages also displayed activity toward tetrathionate, while cells lacking TR1 were unable to reduce tetrathionate. These studies suggest that upregulation of TR1 expression, via selenium supplementation, may modulate the gut microbiome, particularly during inflammation, by regulating the levels of tetrathionate.

Original languageEnglish (US)
Pages (from-to)5121-5124
Number of pages4
JournalBiochemistry
Volume54
Issue number33
DOIs
StatePublished - Aug 25 2015

All Science Journal Classification (ASJC) codes

  • Biochemistry

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