The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)

Amanda S. Hakemian, Christine E. Tinberg, Kalyan C. Kondapalli, Joshua Telser, Brian M. Hoffman, Timothy L. Stemmler*, Amy C. Rosenzweig

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


The oxidation state of copper bound to methanobactin, a small siderophore-like molecule from the methanotroph Methylosinus trichosporium OB3b, was investigated. Purified methanobactin loaded with Cu(II) exhibits a weak EPR signal probably due to adventitious Cu(II). The EPR signal intensity increases significantly upon addition of the strong oxidant nitric acid. Features of the X-ray absorption near edge spectrum, including a 1s → 4p transition at 8985 eV, further indicate the presence of Cu(I). EXAFS data were best fit using a multiple scattering model generated from previously reported crystallographic parameters. These results establish definitively that M. trichosporium OB3b methanobactin binds Cu(I) and suggest that methanobactin itself reduces Cu(II) to Cu(I).

Original languageEnglish (US)
Pages (from-to)17142-17143
Number of pages2
JournalJournal of the American Chemical Society
Issue number49
StatePublished - Dec 14 2005

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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