{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T04:17:07Z","timestamp":1790741827429,"version":"4.1.0"},"reference-count":65,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2021,6,11]],"date-time":"2021-06-11T00:00:00Z","timestamp":1623369600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["R33 ES025645"],"award-info":[{"award-number":["R33 ES025645"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["U01 CA215848"],"award-info":[{"award-number":["U01 CA215848"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["P30 CA012197"],"award-info":[{"award-number":["P30 CA012197"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM072866"],"award-info":[{"award-number":["R01 GM072866"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decamers and disulfide-linked dimers, with the hyperoxidized inactive state (-SO2H) favoring the multimeric structure of the reduced enzyme. Here, we present a study on the structural requirements for the repair of hyperoxidized 2-Cys Prxs by human sulfiredoxin (Srx) and the relative efficacy of physiological reductants hydrogen sulfide (H2S) and glutathione (GSH) in this reaction. The crystal structure of the toroidal Prx1-Srx complex shows an extended active site interface. The loss of this interface within engineered Prx2 and Prx3 dimers yielded variants more resistant to hyperoxidation and repair by Srx. Finally, we reveal for the first time Prx isoform-dependent use of and potential cooperation between GSH and H2S in supporting Srx activity.<\/jats:p>","DOI":"10.3390\/antiox10060946","type":"journal-article","created":{"date-parts":[[2021,6,11]],"date-time":"2021-06-11T12:44:37Z","timestamp":1623415477000},"page":"946","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9266-3925","authenticated-orcid":false,"given":"Tom E.","family":"Forshaw","sequence":"first","affiliation":[{"name":"Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie A.","family":"Reisz","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kimberly J.","family":"Nelson","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajesh","family":"Gumpena","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Reed","family":"Lawson","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas J.","family":"J\u00f6nsson","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanzhi","family":"Wu","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jill E.","family":"Clodfelter","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lynnette C.","family":"Johnson","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cristina M.","family":"Furdui","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"},{"name":"Center for Redox Biology and Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"},{"name":"Comprehensive Cancer Center, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0246-1295","authenticated-orcid":false,"given":"W. Todd","family":"Lowther","sequence":"additional","affiliation":[{"name":"Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"},{"name":"Center for Redox Biology and Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"},{"name":"Comprehensive Cancer Center, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1089\/ars.2010.3624","article-title":"Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins","volume":"15","author":"Hall","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1126\/science.1080405","article-title":"Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling","volume":"300","author":"Wood","year":"2003","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/S0968-0004(02)00003-8","article-title":"Structure, mechanism and regulation of peroxiredoxins","volume":"28","author":"Wood","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.molcel.2012.05.030","article-title":"Feedback control of adrenal steroidogenesis via H2O2-dependent, reversible inactivation of peroxiredoxin III in mitochondria","volume":"46","author":"Kil","year":"2012","journal-title":"Mol. Cell"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.cell.2010.01.009","article-title":"Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling","volume":"140","author":"Woo","year":"2010","journal-title":"Cell"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1089\/ars.2016.6871","article-title":"A peroxidase peroxiredoxin 1-specific redox regulation of the novel FOXO3 microRNA target let-7","volume":"28","author":"Hopkins","year":"2018","journal-title":"Antioxid. Redox Signal."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/nchembio.2536","article-title":"A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation","volume":"14","author":"Maurer","year":"2018","journal-title":"Nat. Chem. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"3107","DOI":"10.1016\/j.celrep.2016.11.071","article-title":"Peroxiredoxin 1 protects telomeres from oxidative damage and preserves telomeric DNA for extension by telomerase","volume":"17","author":"Aeby","year":"2016","journal-title":"Cell Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1101\/gad.313460.118","article-title":"PRDX1 and MTH1 cooperate to prevent ROS-mediated inhibition of telomerase","volume":"32","author":"Ahmed","year":"2018","journal-title":"Genes Dev."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.diff.2017.12.002","article-title":"Impact of oxidative stress on telomere biology","volume":"99","author":"Ahmed","year":"2018","journal-title":"Differentiation"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"e201800121","DOI":"10.26508\/lsa.201800121","article-title":"Transformation-induced stress at telomeres is counteracted through changes in the telomeric proteome including SAMHD1","volume":"1","author":"Majerska","year":"2018","journal-title":"Life Sci. Alliance"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/s00401-008-0373-3","article-title":"Peroxiredoxin 6 in human brain: Molecular forms, cellular distribution and association with Alzheimer\u2019s disease pathology","volume":"115","author":"Power","year":"2008","journal-title":"Acta Neuropathol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"11553","DOI":"10.1038\/s41598-018-29770-3","article-title":"Evidence supporting oxidative stress in a moderately affected area of the brain in Alzheimer\u2019s disease","volume":"8","author":"Youssef","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1590\/1414-431x20144142","article-title":"Peroxiredoxin isoforms are associated with cardiovascular risk factors in type 2 diabetes mellitus","volume":"48","year":"2015","journal-title":"Braz. J. Med. Biol. Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"4843","DOI":"10.1074\/jbc.RA118.006219","article-title":"Pancreatic beta-cells detoxify H2O2 through the peroxiredoxin\/thioredoxin antioxidant system","volume":"294","author":"Stancill","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"6641","DOI":"10.1074\/jbc.M115.693523","article-title":"Oxidative stress promotes peroxiredoxin hyperoxidation and attenuates pro-survival signaling in aging chondrocytes","volume":"291","author":"Collins","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"254","DOI":"10.18632\/aging.100017","article-title":"Identification of Peroxiredoxin 1 as a novel interaction partner for the lifespan regulator protein p66Shc","volume":"1","author":"Gertz","year":"2009","journal-title":"Aging"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1042\/BJ20082003","article-title":"Peroxiredoxin 5 confers protection against oxidative stress and apoptosis and also promotes longevity in Drosophila","volume":"419","author":"Radyuk","year":"2009","journal-title":"Biochem. J."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1177\/1535370216642039","article-title":"Featured Article: Accelerated decline of physical strength in peroxiredoxin-3 knockout mice","volume":"241","author":"Zhang","year":"2016","journal-title":"Exp. Biol. Med."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"S92","DOI":"10.1016\/j.freeradbiomed.2016.10.229","article-title":"Peroxiredoxin-5 as a novel actor in inflammation and tumor suppression","volume":"100","author":"Argyropoulou","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"8038","DOI":"10.1038\/sj.onc.1208821","article-title":"Regulation of reactive oxygen species, DNA damage and c-Myc function by peroxiredoxin 1","volume":"24","author":"Egler","year":"2005","journal-title":"Oncogene"},{"key":"ref_22","first-page":"561","article-title":"Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression","volume":"424","author":"Neumann","year":"2003","journal-title":"Nat. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"e002956","DOI":"10.1161\/JAHA.112.002956","article-title":"Peroxiredoxin 4, a novel circulating biomarker for oxidative stress and the risk of incident cardiovascular disease and all-cause mortality","volume":"1","author":"Abbasi","year":"2012","journal-title":"J. Am. Hear. Assoc."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1002\/1873-3468.12604","article-title":"Prdx1-encoded peroxiredoxin is important for vascular development in zebrafish","volume":"591","author":"Huang","year":"2017","journal-title":"FEBS Lett."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Nelson, K., Messier, T., Milczarek, S., Saaman, A., Beuschel, S., Gandhi, U., Heintz, N., Smalley, T., Lowther, W.T., and Cunniff, B. (2021). Unique cellular and biochemical features of human mitochondrial peroxiredoxin 3 establish the molecular basis for its specific reaction with thiostrepton. Antioxidants, 10.","DOI":"10.3390\/antiox10020150"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1042\/BJ20150572","article-title":"Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation","volume":"473","author":"Poynton","year":"2016","journal-title":"Biochem. J."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"16313","DOI":"10.1073\/pnas.1915275117","article-title":"Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells","volume":"117","author":"Talwar","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"27670","DOI":"10.1016\/S0021-9258(18)47038-X","article-title":"Thioredoxin-dependent peroxide reductase from yeast","volume":"269","author":"Chae","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"29714","DOI":"10.1074\/jbc.M113.473470","article-title":"Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation","volume":"288","author":"Haynes","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"26","DOI":"10.14348\/molcells.2016.2325","article-title":"Kinetic approaches to measuring peroxiredoxin reactivity","volume":"39","author":"Winterbourn","year":"2016","journal-title":"Mol. Cells"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Forshaw, T.E., Holmila, R., Nelson, K.J., Lewis, J.E., Kemp, M.L., Tsang, A.W., Poole, L.B., Lowther, W.T., and Furdui, C.M. (2019). Peroxiredoxins in cancer and response to radiation therapies. Antioxidants, 8.","DOI":"10.3390\/antiox8010011"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"11901","DOI":"10.1074\/jbc.RA117.001690","article-title":"Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins","volume":"293","author":"Bolduc","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3416","DOI":"10.1021\/acs.biochem.8b00188","article-title":"Differential kinetics of two-cysteine peroxiredoxin disulfide formation reveal a novel model for peroxide sensing","volume":"57","author":"Randall","year":"2018","journal-title":"Biochemistry"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1016\/j.str.2005.07.021","article-title":"Bovine mitochondrial peroxiredoxin III forms a two-ring catenane","volume":"13","author":"Cao","year":"2005","journal-title":"Structure"},{"key":"ref_35","first-page":"980","article-title":"ATP-dependent reduction of cysteine\u2013sulphinic acid by S. cerevisiae sulphiredoxin","volume":"425","author":"Biteau","year":"2003","journal-title":"Nat. Cell Biol."},{"key":"ref_36","first-page":"98","article-title":"Structure of the sulphiredoxin\u2013peroxiredoxin complex reveals an essential repair embrace","volume":"451","author":"Johnson","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"33305","DOI":"10.1074\/jbc.M109.036400","article-title":"Protein Engineering of the Quaternary Sulfiredoxin\u00b7peroxiredoxin enzyme-substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation","volume":"284","author":"Johnson","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1089\/ars.2014.5998","article-title":"Evidence that glutathione and the glutathione system efficiently recycle 1-Cys sulfiredoxin in vivo","volume":"22","author":"Boukhenouna","year":"2015","journal-title":"Antioxid. Redox Signal."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1107\/S0907444906045975","article-title":"Solving structures of protein complexes by molecular replacement with Phaser","volume":"63","author":"McCoy","year":"2006","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/S0969-2126(00)00147-7","article-title":"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7\u00c5 resolution","volume":"8","author":"Littlechil","year":"2000","journal-title":"Structure"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: All-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: A program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Collaborative Computational Project (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr., 50, 760\u2013763.","DOI":"10.1107\/S0907444994003112"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"7.10.1","DOI":"10.1002\/0471140856.tx0710s49","article-title":"Measurement of peroxiredoxin activity","volume":"49","author":"Nelson","year":"2011","journal-title":"Curr. Protoc. Toxicol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"10583","DOI":"10.1021\/bi050448i","article-title":"Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin","volume":"44","author":"Parsonage","year":"2005","journal-title":"Biochemistry"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1016\/j.str.2016.04.013","article-title":"Structures of human peroxiredoxin 3 suggest self-chaperoning assembly that maintains catalytic state","volume":"24","author":"Yewdall","year":"2016","journal-title":"Structure"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"50994","DOI":"10.1074\/jbc.M409482200","article-title":"Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine","volume":"279","author":"Chang","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"14400","DOI":"10.1074\/jbc.M511082200","article-title":"Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin","volume":"281","author":"Jeong","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1080\/10715762.2016.1241995","article-title":"Interactions between peroxiredoxin 2, hemichrome and the erythrocyte membrane","volume":"50","author":"Bayer","year":"2016","journal-title":"Free Radic. Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"28873","DOI":"10.1074\/jbc.M804087200","article-title":"Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity","volume":"283","author":"Lim","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"28775","DOI":"10.1074\/jbc.M505362200","article-title":"Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced Cell Death","volume":"280","author":"Moon","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1016\/j.redox.2015.08.011","article-title":"In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation","volume":"6","author":"Noichri","year":"2015","journal-title":"Redox Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1016\/j.biocel.2012.04.008","article-title":"Structural and functional analysis of native peroxiredoxin 2 in human red blood cells","volume":"44","author":"Ogasawara","year":"2012","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"4556","DOI":"10.1016\/j.jmb.2013.09.002","article-title":"Switching between the alternative structures and functions of a 2-Cys peroxiredoxin, by site-directed mutagenesis","volume":"425","author":"Angelucci","year":"2013","journal-title":"J. Mol. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"8470","DOI":"10.1074\/jbc.M808981200","article-title":"Sulfiredoxin translocation into mitochondria plays a crucial role in reducing hyperoxidized peroxiredoxin III","volume":"284","author":"Noh","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.freeradbiomed.2016.10.011","article-title":"Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin: Linking mitochondrial function to circadian rhythm","volume":"100","author":"Rhee","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1038\/s41589-018-0116-2","article-title":"Chemical proteomics reveals new targets of cysteine sulfinic acid reductase","volume":"14","author":"Akter","year":"2018","journal-title":"Nat. Chem. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"22371","DOI":"10.1074\/jbc.M800493200","article-title":"Evidence for the formation of a covalent thiosulfinate intermediate with peroxiredoxin in the catalytic mechanism of sulfiredoxin","volume":"283","author":"Roussel","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"33048","DOI":"10.1074\/jbc.M109.035352","article-title":"Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin","volume":"284","author":"Roussel","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1096\/fj.12-216507","article-title":"Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics","volume":"27","author":"Coletta","year":"2013","journal-title":"FASEB J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"12679","DOI":"10.1073\/pnas.1308487110","article-title":"Oxygen-sensitive mitochondrial accumulation of cystathionine beta-synthase mediated by Lon protease","volume":"110","author":"Teng","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"15466","DOI":"10.1074\/jbc.RA120.014728","article-title":"Acidity and nucleophilic reactivity of glutathione persulfide","volume":"295","author":"Benchoam","year":"2020","journal-title":"J. Biol. Chem."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/10\/6\/946\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:13:14Z","timestamp":1760163194000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/10\/6\/946"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6,11]]},"references-count":65,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2021,6]]}},"alternative-id":["antiox10060946"],"URL":"https:\/\/doi.org\/10.3390\/antiox10060946","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,6,11]]}}}