The sixteenth iron in the nitrogenase MoFe protein

Limei Zhang, Jens T. Kaiser, Gabriele Meloni, Kun Yun Yang, Thomas Spatzal, Susana L.A. Andrade, Oliver Einsle, James B. Howard, Douglas C. Rees

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Another iron in the fire: X-ray anomalous diffraction studies on the nitrogenase MoFe protein show the presence of a mononuclear iron site, designated as Fe16, which was previously identified as either Ca2+ or Mg2+. The position of the absorption edge indicates that this site is in the oxidation state +2. The high sequence conservation of the residues coordinated to Fe16 emphasizes the potential importance of the site in nitrogenase.

Original languageEnglish (US)
Pages (from-to)10529-10532
Number of pages4
JournalAngewandte Chemie - International Edition
Volume52
Issue number40
DOIs
StatePublished - Sep 27 2013

Keywords

  • iron
  • metalloproteins
  • multiple-wavelength anomalous diffraction
  • nitrogen fixation
  • nitrogenases

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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