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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,7,28]]},"abstract":"<jats:p>\n                    Hydrogen sulfide (H\n                    <jats:sub>2<\/jats:sub>\n                    S) functions as a gaseous signaling molecule in plant stress responses through the persulfidation of protein cysteine (Cys) residues. A comprehensive, Cys site-specific map of the plant persulfidome has been lacking, despite its importance for achieving a systems-level understanding of the biological roles of Cys persulfidation. Using a state-of-the-art\n                    <jats:italic toggle=\"yes\">N<\/jats:italic>\n                    -ethylmaleimide-biotin-based proteomics strategy, we generate a dynamic map of 1,691 persulfidated Cys sites in the rice (\n                    <jats:italic toggle=\"yes\">Oryza sativa<\/jats:italic>\n                    ) leaf proteome. Our results reveal a global dynamic changes in protein persulfidation during prolonged salt stress, with notable impacts on proteins involved in metal-dependent catalysis, redox metabolism, and the pentose phosphate pathway (PPP). Based on these patterns, we investigated the functional relevance of persulfidation within the nonoxidative PPP. H\n                    <jats:sub>2<\/jats:sub>\n                    S-mediated persulfidation decreased the activity of the representative nonoxidative PPP enzyme ribose-5-phosphate isomerase, leading to increased NADPH production and subsequent activation of NADPH-dependent redox enzymes, including monodehydroascorbate reductase (MDHAR) isoforms of the ascorbate-glutathione (AsA-GSH) cycle. Persulfidation protected MDHAR3\/5 from oxidative inhibition and degradation, thereby sustaining AsA-GSH cycle capacity and supporting reactive oxygen species scavenging. This site-specific persulfidome provides a valuable resource for exploring plant redox regulation, and our functional analyses offer mechanistic insight into how H\n                    <jats:sub>2<\/jats:sub>\n                    S-dependent protein persulfidation modulates redox metabolic fluxes to bolster NADPH availability and maintain redox homeostasis during salt-stress adaptation.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2608150123","type":"journal-article","created":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T18:00:45Z","timestamp":1784656845000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":2,"title":["H\n                    <sub>2<\/sub>\n                    S-mediated protein persulfidation regulates redox metabolic flux underlying salt-stress resilience in 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