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The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a biologically unprecedented μ(6)-coordinated C(4-) ion. Although the role of this interstitial atom in nitrogenase catalysis is unknown, progress in understanding its biosynthetic origins has been made. Here we report valence-to-core Fe Kβ X-ray emission spectroscopy data to show that this C(4-) ion is present in the Fe(8)S(9) "L-cluster," which is the immediate precursor to FeMoco prior to the insertion of molybdenum and coordination by homocitrate. These results accord with recent evidence supporting a role for the S-adenosylmethionine-dependent enzyme NifB in the incorporation of carbon into the FeMoco center of nitrogenase.


Kyle M Lancaster, Yilin Hu, Uwe Bergmann, Markus W Ribbe, Serena DeBeer. X-ray spectroscopic observation of an interstitial carbide in NifEN-bound FeMoco precursor. Journal of the American Chemical Society. 2013 Jan 16;135(2):610-2

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PMID: 23276198

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