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DJ\u20101 protects against oxidative damage and mitochondrial dysfunction through a homeostatic control of reactive oxygen species (ROS). DJ\u20101 pathology results from a loss of function, where ROS readily oxidizes a highly conserved and functionally essential cysteine (C106). The over\u2010oxidation of DJ\u20101 C106 leads to a dynamically destabilized and biologically inactivated protein. An analysis of the structural stability of DJ\u20101 as a function of oxidative state and temperature may provide further insights into the role the protein plays in PD progression. NMR spectroscopy, circular dichroism, analytical ultracentrifugation sedimentation equilibrium, and molecular dynamics simulations were utilized to investigate the structure and dynamics of the reduced, oxidized (C106\u2010SO<jats:sub>2<\/jats:sub><jats:sup>\u2212<\/jats:sup>), and over\u2010oxidized (C106\u2010SO<jats:sub>3<\/jats:sub><jats:sup>\u2212<\/jats:sup>) forms of DJ\u20101 for temperatures ranging from 5\u00b0C to 37\u00b0C. The three oxidative states of DJ\u20101 exhibited distinct temperature\u2010dependent structural changes. A cold\u2010induced aggregation occurred for the three DJ\u20101 oxidative states by 5\u00b0C, where the over\u2010oxidized state aggregated at significantly higher temperatures than both the oxidized and reduced forms. Only the oxidized and over\u2010oxidized forms of DJ\u20101 exhibited a mix state containing both folded and partially denatured protein that likely preserved secondary structure content. The relative amount of this denatured form of DJ\u20101 increased as the temperature was lowered, consistent with a cold\u2010denaturation. Notably, the cold\u2010induced aggregation and denaturation for the DJ\u20101 oxidative states were completely reversible. The dramatic changes in the structural stability of DJ\u20101 as a function of oxidative state and temperature are relevant to its role in PD and its functional response to oxidative stress.<\/jats:p>","DOI":"10.1002\/bip.23534","type":"journal-article","created":{"date-parts":[[2023,3,27]],"date-time":"2023-03-27T17:59:26Z","timestamp":1679939966000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["The reversible low\u2010temperature instability of human DJ\u20101 oxidative states"],"prefix":"10.1002","volume":"115","author":[{"given":"Tessa","family":"Andrews","sequence":"first","affiliation":[{"name":"Department of Chemistry University of Nebraska\u2010Lincoln  Lincoln Nebraska 68588\u20100304 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Javier","family":"Seravallic","sequence":"additional","affiliation":[{"name":"Department of Biochemistry University of Nebraska\u2010Lincoln  Lincoln Nebraska 68588\u20100664 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9948-6837","authenticated-orcid":false,"given":"Robert","family":"Powers","sequence":"additional","affiliation":[{"name":"Department of Chemistry University of Nebraska\u2010Lincoln  Lincoln Nebraska 68588\u20100304 USA"},{"name":"Redox Biology Center University of Nebraska\u2010Lincoln  Lincoln Nebraska 68588\u20100664 USA"},{"name":"Nebraska Center for Integrated Biomolecular Communication University of Nebraska\u2010Lincoln  Lincoln Nebraska 68588\u20100304 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2023,3,27]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature02261"},{"key":"e_1_2_10_3_1","first-page":"223","volume":"181","author":"Anfinsen C.","year":"1973","journal-title":"B."},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1080\/07391102.2015.1073631"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms231810798"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1063\/1.4947493"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr960383c"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0811922106"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2021.642623"},{"key":"e_1_2_10_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41580-019-0133-3"},{"key":"e_1_2_10_11_1","doi-asserted-by":"publisher","DOI":"10.1093\/jb\/mvp139"},{"key":"e_1_2_10_12_1","doi-asserted-by":"publisher","DOI":"10.3109\/10409239009090612"},{"key":"e_1_2_10_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpc.2015.05.007"},{"key":"e_1_2_10_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41593-018-0235-9"},{"key":"e_1_2_10_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2013.01.018"},{"key":"e_1_2_10_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0896-6273(03)00568-3"},{"key":"e_1_2_10_17_1","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.2000.4262"},{"key":"e_1_2_10_18_1","doi-asserted-by":"publisher","DOI":"10.1002\/humu.21277"},{"key":"e_1_2_10_19_1","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1997.6132"},{"key":"e_1_2_10_20_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1077209"},{"key":"e_1_2_10_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2009.08.003"},{"key":"e_1_2_10_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2017.08.005"},{"key":"e_1_2_10_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(03)00764-6"},{"key":"e_1_2_10_24_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M304221200"},{"key":"e_1_2_10_25_1","first-page":"1","volume":"4","author":"Trempe J.\u2010F.","year":"2013","journal-title":"Front. 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