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Rice, Derek
Max Planck Institute for Chemical Energy Conversion
in Cooperation with on an Cooperation-Score of 37%
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article
An Fe6C Core in All Nitrogenase Cofactors
Abstract
<jats:title>Abstract</jats:title><jats:p>The biological process of dinitrogen reduction to ammonium occurs at the cofactors of nitrogenases, the only enzymes that catalyze this challenging chemical reaction. Three types of nitrogenases have been described, named according to the heterometal in their cofactor: molybdenum, vanadium or iron nitrogenases. Spectroscopic and structural characterization allowed the unambiguous identification of the cofactors of molybdenum and vanadium nitrogenases and revealed a central μ<jats:sub>6</jats:sub>‐carbide in both of them. Although genetic studies suggested that the cofactor of the iron nitrogenase contains a similar Fe<jats:sub>6</jats:sub>C core, this has not been experimentally demonstrated. Here we report Valence‐to‐Core X‐ray Emission Spectroscopy providing experimental evidence that this cofactor contains a carbide, thereby making the Fe<jats:sub>6</jats:sub>C core a feature of all nitrogenase cofactors.</jats:p>