{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T16:04:43Z","timestamp":1790006683223,"version":"4.0.1"},"reference-count":63,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T00:00:00Z","timestamp":1789948800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T00:00:00Z","timestamp":1789948800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Angew Chem Int Ed"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Hydropersulfides have gained attention as excellent biochemical nucleophiles and membrane\u2010protective radical scavengers. They form perthiyl radicals, which terminate radical chain reactions through self\u2010recombination, yielding polysulfides. It is currently unknown exactly how polysulfides are subsequently reduced. Using stopped\u2013flow kinetic measurements in combination with mass spectrometry, we show that the model class I glutaredoxin from\n                    <jats:italic>Plasmodium falciparum<\/jats:italic>\n                    (PfGrx) rapidly reduces the polysulfides glutathione trisulfide (GS\n                    <jats:sub>3<\/jats:sub>\n                    G) and tetrasulfide (GS\n                    <jats:sub>4<\/jats:sub>\n                    G), yielding glutathionylated PfGrx and the corresponding glutathione hydropersulfide (GSSH) and hydrotrisulfide (GS\n                    <jats:sub>3<\/jats:sub>\n                    H). The second\u2010order rate constants of these reductions \u226510\n                    <jats:sup>7<\/jats:sup>\n                    M\n                    <jats:sup>\u22121<\/jats:sup>\n                    s\n                    <jats:sup>\u22121<\/jats:sup>\n                    are even slightly higher than for glutathione disulfide (GSSG). In contrast, PfGrx was inactive or only moderately active toward cystine or cysteine trisulfide. GSSH and GS\n                    <jats:sub>3<\/jats:sub>\n                    H are further reduced by PfGrx with second\u2010order rate constants on the order of 10\n                    <jats:sup>6\u2212<\/jats:sup>\n                    10\n                    <jats:sup>7<\/jats:sup>\n                    M\n                    <jats:sup>\u22121<\/jats:sup>\n                    s\n                    <jats:sup>\u22121<\/jats:sup>\n                    , yielding glutathionylated PfGrx and hydrogen sulfide (H\n                    <jats:sub>2<\/jats:sub>\n                    S) or hydrogen disulfide (H\n                    <jats:sub>2<\/jats:sub>\n                    S\n                    <jats:sub>2<\/jats:sub>\n                    ), respectively. Thus, glutaredoxins specifically recognize the glutathione moiety of glutathione (hydro)per\/polysulfides. Since reduced glutathione (GSH) rapidly reduces glutathionylated glutaredoxins, glutathione (hydro)per\/polysulfides are efficiently converted to GSSG and H\n                    <jats:sub>2<\/jats:sub>\n                    S or the corresponding hydrogen polysulfides. As a consequence, the steady\u2010state concentration of glutathione (hydro)per\/polysulfides should be tightly controlled in subcellular compartments containing active glutaredoxins and high GSH concentrations.\n                  <\/jats:p>","DOI":"10.1002\/anie.1222129","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T15:27:41Z","timestamp":1790004461000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Glutaredoxins Rapidly Reduce Glutathione Hydroper\u2010 and Polysulfides"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-4512-4424","authenticated-orcid":false,"given":"Philipp","family":"Reinert","sequence":"first","affiliation":[{"name":"Department of Chemistry Comparative Biochemistry RPTU Kaiserslautern  Kaiserslautern 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Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0623-1710","authenticated-orcid":false,"given":"Takaaki","family":"Akaike","sequence":"additional","affiliation":[{"name":"Department of Redox Molecular Medicine Tohoku University Graduate School of Medicine  Sendai Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8426-166X","authenticated-orcid":false,"given":"Uladzimir","family":"Barayeu","sequence":"additional","affiliation":[{"name":"Max\u2010Planck\u2010Institute for Polymer Research  Mainz Germany"},{"name":"Department of Redox Molecular Medicine Tohoku University Graduate School of Medicine  Sendai Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2141-917X","authenticated-orcid":false,"given":"Marcel","family":"Deponte","sequence":"additional","affiliation":[{"name":"Department of Chemistry Comparative Biochemistry RPTU Kaiserslautern  Kaiserslautern 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