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Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation

descriptionPublicationkeyboard_double_arrow_right Article , Other literature type 01 Jan 2016 United Kingdom, Germany, Serbia, United States Publisher:Royal Society of Chemistry (RSC)Journal:Chemical Science, volume 7, pages 3,414-3,426 (issn: 2041-6520, eissn: 2041-6539,

Copyright policy )Funded by:NIH | Novel Sulfide Releasing A..., NIH | Enzymology of H2S Biogene..., NIH | Enzymology of Sulfide Oxi... +1 projects

Authors: Isao Ishii; Ellen G. Harrer; Pramod Kumar Yadav; Erwan Galardon; Mark E. Wood; Shengwei Wei; Ruma Banerjee; +15 Authors

doi: 10.1039/c5sc04818d

pmid: 27170841

pmc: PMC4845716

handle: 10871/20249

Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation

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Abstract

H2S signalsviaprotein persulfidation. To be regulatory the modification will have to be reversible. Using a new method for persulfide detection, we discover this missing link and show that thioredoxin system acts as depersulfidasein vivo.

Countries

United Kingdom, Germany, Serbia, United States

Related Organizations

University of Bordeaux
France
CNRS
France
Washington State University
United States
Friedrich-Alexander-Universität Erlangen-Nürnberg
Centre National de la Recherche Scientifique
France

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Keywords

Chemistry, Cardiovascular and Metabolic Diseases, 610, -, Naturwissenschaftliche Fakultät, 540, ddc: ddc:540

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