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X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor

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Neese,  Frank
Institut für Physikalische und Theoretische Chemie, Universität Bonn, Wegelerstr. 12, D-53115 Bonn, Germany;
Research Department Neese, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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DeBeer,  Serena
Department of Chemistry and Chemical Biology, Cornell University;
Research Department Neese, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Citation

Lancaster, K. M., Roemelt, M., Ettenhuber, P., Hu, Y., Ribbe, M. W., Neese, F., et al. (2011). X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor. Science, 334(6058), 974-977. doi:10.1126/science.1206445.


Cite as: http://hdl.handle.net/21.11116/0000-0007-FF6B-3
Abstract
Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient ∆nifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C4–. Identification of the central atom will drive further studies on its role in catalysis.