2014/08/01 by Philipp P. Hallmen, Johannes Kästner · 1 citation
Energy · Chemical Engineering · Materials Science · #Metalloenzymes and iron-sulfur proteins #Ammonia Synthesis and Nitrogen Reduction #Hydrogen Storage and Materials
paper · doi:10.1002/zaac.201400114
openalex publication_date 2014/08/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/23
Abstract Nitrogenase converts gaseous dinitrogen into biologically accessible ammonia. The binding of N 2 to a reduced and protonated form of the FeMo‐cofactor of nitrogenase including its central carbon ligand was investigated by means of density functional calculations. It was found the central ligand to stabilize the cluster. N 2 can associate to iron or molybdenum with iron being the preferred binding site. While endo and exo binding modes were investigated the exo modes are more stable. Implications on the mechanism of N 2 reduction are discussed.