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Published September 27, 2013 | Accepted Version
Journal Article Open

The Sixteenth Iron in the Nitrogenase MoFe Protein


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.

Additional Information

© 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Received: May 6, 2013. Published online: August 21, 2013. The work was supported by the NIH (grant GM45162 to D.C.R.), NSERC PDF award (to L.M.Z.), and Deutsche Forschungsgemeinschaft (grants Ei-520/7 to O.E., An-676/1 to S.L.A.A., and IRTG 1478). G.M. is a Marie Curie International Outgoing Fellow (European Commission, grant no. 252961). We thank staff at Beamline 12–2, Stanford Synchrotron Radiation Lightsource (SSRL) and staff at HXMA Beamline, Canada Light Source (CLS). SSRL is operated for the DOE and supported by its OBER and by the NIH, NIGMS (P41GM103393) and the NCRR (P41RR001209). CLS is supported by NSERC, NRC, CIHR, and the University of Saskatchewan. We acknowledge the Gordon and Betty Moore Foundation, the Beckman Institute, and the Sanofi-Aventis Bioengineering Research Program at Caltech for their generous support of the Molecular Observatory at Caltech. The assistance of Nathan Dalleska and the resources of the Caltech Environmental Analysis Center are greatly appreciated.

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Accepted Version - nihms-534176.pdf


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