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@ARTICLE{Zimmermann:294765,
      author       = {J. Zimmermann and L. Lang and G. Calabrese and H. Laporte
                      and P. S. Amponsah and C. Michalk and T. Sukmann and J.
                      Oestreicher and A. Tursch and E. Peker and T. N. E.
                      Owusu$^*$ and M. Weith and L. P. Roma and M. Deponte and J.
                      Riemer and B. Morgan},
      title        = {{T}sa1 is the dominant peroxide scavenger and a source of
                      {H}2{O}2-dependent {GSSG} production in yeast.},
      journal      = {Free radical biology and medicine},
      volume       = {226},
      issn         = {0891-5849},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2024-02480},
      pages        = {408 - 420},
      year         = {2025},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {Hydrogen peroxide (H2O2) is an important biological
                      molecule, functioning both as a second messenger in cell
                      signaling and, especially at higher concentrations, as a
                      cause of cell damage. Cells harbor multiple enzymes that
                      have peroxide reducing activity in vitro. However, the
                      contribution of each of these enzymes towards peroxide
                      scavenging in vivo is less clear. Therefore, to directly
                      investigate in vivo peroxide scavenging, we used the
                      genetically encoded peroxide probes, roGFP2-Tsa2ΔCR and
                      HyPer7, to systematically screen the peroxide scavenging
                      capacity of baker's yeast thiol and heme peroxidase mutants.
                      We show that the 2-Cys peroxiredoxin Tsa1 alone is
                      responsible for almost all exogenous H2O2 and tert-butyl
                      hydroperoxide scavenging. Furthermore, Tsa1 can become an
                      important source of H2O2-dependent cytosolic glutathione
                      disulfide production. The two catalases and cytochrome c
                      peroxidase only produce observable scavenging defects at
                      higher H2O2 concentrations when these three heme peroxidases
                      are removed in combination. We also analyzed the reduction
                      of Tsa1 in vitro, revealing that the enzyme is efficiently
                      reduced by thioredoxin-1 with a rate constant of 2.8 × 106
                      M-1s-1 but not by glutaredoxin-2. Tsa1 reduction by reduced
                      glutathione occurs nonenzymatically with a rate constant of
                      2.9 M-1s-1. Hence, the observed Tsa1-dependent glutathione
                      disulfide production in yeast probably requires the
                      oxidation of thioredoxins. Our findings clarify the
                      importance of the various thiol and heme peroxidases for
                      peroxide removal and suggest that most thiol peroxidases
                      have alternative or specialized functions in specific
                      subcellular compartments.},
      keywords     = {Catalase (Other) / H(2)O(2) scavenging (Other) / Heme
                      peroxidase (Other) / HyPer7 (Other) / Peroxiredoxin (Other)
                      / Thiol peroxidase (Other) / roGFP2 (Other)},
      cin          = {A160},
      ddc          = {610},
      cid          = {I:(DE-He78)A160-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39515595},
      doi          = {10.1016/j.freeradbiomed.2024.11.004},
      url          = {https://inrepo02.dkfz.de/record/294765},
}