文摘
The iron鈥搈olybdenum cofactor (FeMoco) of nitrogenase contains a biologically unprecedented 渭6-coordinated C4鈥?/sup> 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 K尾 X-ray emission spectroscopy data to show that this C4鈥?/sup> ion is present in the Fe8S9 鈥淟-cluster,鈥?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.