Reduction of Tetrathionate by Mammalian Thioredoxin Reductase

Vivek Narayan, Avinash K. Kudva, Kumble Sandeep Prabhu

Research output: Contribution to journalArticle

4 Citations (Scopus)

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

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Thioredoxin-Disulfide Reductase
Selenium
Hydrogen Sulfide
Salmonella
Macrophages
Enterobacteriaceae
Liver
Rats
Reactive Oxygen Species
Up-Regulation
Electrons
Inflammation
Oxidation
Growth
Gastrointestinal Microbiome
In Vitro Techniques
polythionates

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Narayan, Vivek ; Kudva, Avinash K. ; Prabhu, Kumble Sandeep. / Reduction of Tetrathionate by Mammalian Thioredoxin Reductase. In: Biochemistry. 2015 ; Vol. 54, No. 33. pp. 5121-5124.
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Reduction of Tetrathionate by Mammalian Thioredoxin Reductase. / Narayan, Vivek; Kudva, Avinash K.; Prabhu, Kumble Sandeep.

In: Biochemistry, Vol. 54, No. 33, 25.08.2015, p. 5121-5124.

Research output: Contribution to journalArticle

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AB - 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.

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