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We investigated these antioxidant systems in\n                      <jats:italic toggle=\"yes\">Borrelia burgdorferi<\/jats:italic>\n                      , the Mn-accumulating, Fe-independent Lyme disease pathogen. Using electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR) spectroscopies, we tracked Mn\u00b2\n                      <jats:sup>+<\/jats:sup>\n                      partitioning between enzyme-bound (L-Mn) and metabolite-bound (H-Mn) pools in spirochetes at exponential and stationary phases. Results show that MnSOD neutralizes extracellular O\n                      <jats:sub>2<\/jats:sub>\n                      <jats:sup>\u2022\u2212<\/jats:sup>\n                      generated by \u03b3-irradiation (a model for host immune attack); H-Mn neutralizes cytoplasmic O\n                      <jats:sub>2<\/jats:sub>\n                      <jats:sup>\u2022\u2212<\/jats:sup>\n                      and is a reservoir of labile Mn\u00b2\n                      <jats:sup>+<\/jats:sup>\n                      for metalating Mn-dependent enzymes. MnCl\n                      <jats:sub>2<\/jats:sub>\n                      supplementation in log phase\n                      <jats:italic toggle=\"yes\">B. burgdorferi<\/jats:italic>\n                      restored radioresistance in \u0394MnSOD mutants via H-Mn hyperaccumulation but induced toxicity in older, stationary phase cells as metabolites became depleted. These findings support an expanded oxidative-stress model in which H-Mn complements MnSOD and positions Mn homeostasis as a therapeutic target. Our approach highlights the utility of EPR and ENDOR in studying Mn-dependent pathogens.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        We employed electron paramagnetic resonance and electron-nuclear double resonance spectroscopies of Mn\u00b2\n                        <jats:sup>+<\/jats:sup>\n                        in intact\n                        <jats:italic toggle=\"yes\">Borrelia burgdorferi<\/jats:italic>\n                        supplemented with MnCl\n                        <jats:sub>2<\/jats:sub>\n                        to track changes in the amounts of enzyme-bound Mn and substitutionally labile, antioxidant Mn-metabolite complexes. We measured the spirochete\u2019s survivability to acute \u03b3-irradiation, which simulates the respiratory burst of O\n                        <jats:sub>2<\/jats:sub>\n                        <jats:sup>\u2022\u2212<\/jats:sup>\n                        deployed as a critical weapon in the host\u2019s innate immune response. While Mn-superoxide dismutase (MnSOD) has classically been viewed as the main defense against oxidative damage in\n                        <jats:italic toggle=\"yes\">B. burgdorferi<\/jats:italic>\n                        , our study demonstrates that antioxidant Mn\n                        <jats:sup>2+<\/jats:sup>\n                        complexes with the metabolite components of H-Mn play a crucial antioxidant role, particularly when MnSOD is deficient. However,\n                        <jats:italic toggle=\"yes\">B. burgdorferi\u2019s<\/jats:italic>\n                        inability to safely store excess Mn in metabolite-depleted cells highlights novel metabolic vulnerabilities that could be exploited for managing Lyme disease.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.02824-25","type":"journal-article","created":{"date-parts":[[2025,11,13]],"date-time":"2025-11-13T14:00:14Z","timestamp":1763042414000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["EPR spectroscopy reveals antioxidant manganese defenses in the Lyme disease pathogen\n                    <i>Borrelia burgdorferi<\/i>"],"prefix":"10.1128","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4703-1387","authenticated-orcid":false,"given":"Andr\u00e9s F.","family":"Londo\u00f1o","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/04r3kq386","id-type":"ROR","asserted-by":"publisher"}],"name":"School of Medicine, Uniformed Services University of the Health Sciences (USUHS)","place":["Bethesda, USA"]},{"name":"Henry M. 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