Fluoride-dependent conversion of organic compounds mediated by manganese peroxidases in the absence of Mn2+ ions

Research output: Contribution to journalResearch articleContributedpeer-review


  • Lidan Ye - , Friedrich Schiller University Jena (Author)
  • Dieter Spiteller - , Max Planck Institute for Chemical Ecology (Author)
  • René Ullrich - , Chair of Environmental Biotechnology (Author)
  • Wilhelm Boland - , Max Planck Institute for Chemical Ecology (Author)
  • Jörg Nüske - , Friedrich Schiller University Jena (Author)
  • Gabriele Diekert - , Friedrich Schiller University Jena (Author)


Manganese peroxidase generally mediates the oxidation of Mn2+ to Mn3+ with H2O2 as an oxidant. Several manganese peroxidases purified from different lignin-degrading fungi were found to mediate a fluoride-dependent conversion of organic substrates such as monochlorodimedone or 2,6-dimethoxyphenol in the absence of manganese ions. Using the manganese peroxidase MnP-1 from Bjerkandera adusta strain Ud1, these fluoride-dependent reactions were studied with respect to different substrates converted, reaction products, and kinetic properties to shed some light on the reaction mechanism of manganese peroxidase. The analysis of the reaction products formed from monochlorodimedone and 2,6-dimethoxyphenol showed that the substrates were oxidized rather than fluorinated. The addition of fluoride to MnP-1 resulted in altered absorption spectra, indicating a coordinative binding of fluoride or HF to the heme iron; the fluoride:heme stoichiometry was determined to be 1:1 and the KD value to be ∼2.5 mM at pH 3.4. The high KD value indicates weak binding of fluoride to the heme. Fluoride appeared to act as a partially competitive inhibitor with respect to hydrogen peroxide for binding to the heme as the sixth ligand. From the findings, a putative model for the fluoride-dependent reaction was developed. The data were interpreted to indicate that changes of the reaction center of manganese peroxidase as, for example, caused by fluoride binding may lead to the oxidation of organic compounds in the absence of manganese by opening a long-range electron transfer pathway.


Original languageEnglish
Pages (from-to)7264-7271
Number of pages8
Journal Biochemistry : a weekly publication of the American Chemical Society
Issue number34
Publication statusPublished - 28 Jul 2010

External IDs

PubMed 20666406


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