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dc.contributor.authorVitvitsky, V
dc.contributor.authorMiljkovic, JL
dc.contributor.authorBostelaar, T
dc.contributor.authorAdhikari, B
dc.contributor.authorYadav, PK
dc.contributor.authorSteiger, AK
dc.contributor.authorTorregrossa, R
dc.contributor.authorPluth, MD
dc.contributor.authorWhiteman, M
dc.contributor.authorBanerjee, R
dc.contributor.authorFilipovic, MR
dc.date.accessioned2018-07-31T11:16:08Z
dc.date.issued2018-07-18
dc.description.abstractHydrogen sulfide (H2S) is an endogenously produced gas that is toxic at high concentrations. It is eliminated by a dedicated mitochondrial sulfide oxidation pathway, which connects to the electron transfer chain at the level of complex III. Direct reduction of cytochrome c (Cyt C) by H2S has been reported previously but not characterized. In this study, we demonstrate that reduction of ferric Cyt C by H2S exhibits hysteretic behavior, which suggests the involvement of reactive sulfur species in the reduction process and is consistent with a reaction stoichiometry of 1.5 mol of Cyt C reduced/mol of H2S oxidized. H2S increases O2 consumption by human cells (HT29 and HepG2) treated with the complex III inhibitor antimycin A, which is consistent with the entry of sulfide-derived electrons at the level of complex IV. Cyt C-dependent H2S oxidation stimulated protein persulfidation in vitro, while silencing of Cyt C expression decreased mitochondrial protein persulfidation in a cell culture. Cyt C released during apoptosis was correlated with persulfidation of procaspase 9 and with loss of its activity. These results reveal a potential role for the electron transfer chain in general, and Cyt C in particular, for potentiating sulfide-based signaling.en_GB
dc.description.sponsorshipThis work was supported by the French State in the frame of the “Investments for the future” Programme IdEx Bordeaux, reference ANR-10-IDEX-03-02, and by an ATIP-AVENIR grant (to M.R.F.), the National Institutes of Health (GM112455 to R.B. and R01GM113030 to M.D.P.), the Medical Research Council, UK (MR/M022706/1 to M.W.), the National Science Foundation (DGE-1309047 to A.K.S.), and the Brian Ridge Scholarship (R.T.). The authors are grateful to M.-F. Giraud for the help with purification of mitochondria.en_GB
dc.identifier.citationPublished online 2 July 2018en_GB
dc.identifier.doi10.1021/acschembio.8b00463
dc.identifier.urihttp://hdl.handle.net/10871/33604
dc.language.isoenen_GB
dc.publisherAmerican Chemical Societyen_GB
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pubmed/29966080en_GB
dc.rights.embargoreasonUnder embargo until 2 July 2019 in compliance with publisher policy.en_GB
dc.rights© 2018. American Chemical Society, All rights reserved.en_GB
dc.titleCytochrome c Reduction by H2S Potentiates Sulfide Signaling.en_GB
dc.typeArticleen_GB
exeter.place-of-publicationUnited Statesen_GB
dc.descriptionThis is the author accepted manuscript. The final version is available from American Chemical Society via the DOI in this record.en_GB
dc.identifier.journalACS Chemical Biologyen_GB


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