title: The sixteenth iron in the nitrogenase MoFe protein.
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 Ca(2+) or Mg(2+). 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.
authors: Division of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125 (USA).
authors: Limei
authors: L
authors: Zhang
authors: Jens T
authors: JT
authors: Kaiser
authors: Gabriele
authors: G
authors: Meloni
authors: Kun-Yun
authors: KY
authors: Yang
authors: Thomas
authors: T
authors: Spatzal
authors: Susana L A
authors: SL
authors: Andrade
authors: Oliver
authors: O
authors: Einsle
authors: James B
authors: JB
authors: Howard
authors: Douglas C
authors: DC
authors: Rees
mesh_terms: D018360:Crystallography, X-Ray; D007501:Iron / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008983:Molybdoferredoxin / Q000737:chemistry* / Q000378:metabolism; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D008983:Molybdoferredoxin; D007501:Iron; D009591:Nitrogenase
keywords: iron; metalloproteins; multiple-wavelength anomalous diffraction; nitrogen fixation; nitrogenases
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