1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum

M.L. Ganadu, F. Bonomi, S. Pagani, R. Boelens

Research output: Contribution to journalArticleAcademicpeer-review


The 8Fe-8S ferredoxin from Clostridium pasteurianum was investigated by 1D and 2D 1H NMR. Spectra of a well-structured, full native preparation of the oxidized protein in 1 M NaCl at pH 8.0 are presented. Assignments of non-isotropically shifted resonances in the diamagnetic region of the spectrum, namely those of the unique aromatic residues F30 and Y2, are presented for the first time.
Original languageEnglish
Pages (from-to)577-585
Number of pages9
JournalBiochemistry International
Issue number4
Publication statusPublished - 20 Jan 1992


  • ferredoxin
  • phenylalanine
  • tyrosine
  • article
  • Clostridium pasteurianum
  • nonhuman
  • priority journal
  • protein structure
  • proton nuclear magnetic resonance


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