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@ARTICLE{Belikova:7755,
      author       = {Belikova, N.A. and Tyurina, Y.Y. and Borisenko, G. and
                      Tyurin, V. and Samhan Arias, A.K. and Yanamala, N. and
                      Furtmüller, P.G. and Klein-Seetharaman, J. and Obinger, C.
                      and Kagan, V.E.},
      title        = {{H}eterolytic reduction of fatty acid hydroperoxides by
                      cytochrome c/cardiolipin complexes: antioxidant function in
                      mitochondria},
      journal      = {Journal of the American Chemical Society},
      volume       = {131},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-7755},
      pages        = {11288 - 11289},
      year         = {2009},
      note         = {This work was supported by grants from the NIH
                      (U19-AI068021, HL70755, R03TW007320, 2RO1LM007994-05), the
                      NSF (CC0449117), the PittGrid, and la Junta de Extremadura,
                      Orden 2008050288 (A.K.S.A.).},
      abstract     = {Cytochrome c (cyt c), a mitochondrial intermembrane
                      electron shuttle between complexes III and IV, can, upon
                      binding with an anionic phospholipid, cardiolipin (CL), act
                      as a peroxidase that catalyzes cardiolipin oxidation.
                      H(2)O(2) was considered as a source of oxidative equivalents
                      for this reaction, which is essential for programmed cell
                      death. Here we report that peroxidase cyt c/CL complexes can
                      utilize free fatty acid hydroperoxides (FFA-OOH) at
                      exceptionally high rates that are approximately 3 orders of
                      magnitude higher than for H(2)O(2). Similarly, peroxidase
                      activity of murine liver mitochondria was high with FFA-OOH.
                      Using EPR spin trapping and LC-MS techniques, we have
                      demonstrated that cyt c/CL complexes split FFA-OOH
                      predominantly via a heterolytic mechanism, yielding
                      hydroxy-fatty acids, whereas H(2)O(2) (and tert-butyl
                      hydroperoxide, t-BuOOH) undergo homolytic cleavage. Computer
                      simulations have revealed that Arg(38) and His(33) are
                      important for the heterolytic mechanism at potential FFA-OOH
                      binding sites of cyt c (but not for H(2)O(2) or t-BuOOH).
                      Regulation of FFA-OOH metabolism may be an important
                      function of cyt c that is associated with elimination of
                      toxic FFA-OOH and synthesis of physiologically active
                      hydroxy-fatty acids in mitochondria.},
      keywords     = {Animals / Antioxidants: metabolism / Armoracia: enzymology
                      / Cardiolipins: metabolism / Cytochromes c: metabolism /
                      Fatty Acids: metabolism / Hydrogen Peroxide: metabolism /
                      Mitochondria, Liver: enzymology / Models, Molecular /
                      Murinae / Oxidation-Reduction / Protein Binding /
                      Antioxidants (NLM Chemicals) / Cardiolipins (NLM Chemicals)
                      / Fatty Acids (NLM Chemicals) / Hydrogen Peroxide (NLM
                      Chemicals) / Cytochromes c (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Chemistry, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19627079},
      UT           = {WOS:000269379200009},
      doi          = {10.1021/ja904343c},
      url          = {https://juser.fz-juelich.de/record/7755},
}