N2 Binding to the FeMo‐Cofactor of Nitrogenase1. Issue 1 (1st August 2014)

• Record Type: Journal Article
• Authors: Hallmen, Philipp P.; Kästner, Johannes
• Is Part Of: Zeitschrift für anorganische und allgemeine Chemie. Volume 641:Issue 1(2015)
• Page Start: 118
• Page End: 122
• Publication Date: 2014-08-01
• Subjects: Chemistry, Inorganic -- Periodicals; Chemistry -- Periodicals; 540
• DOI: 10.1002/zaac.201400114
• Languages: English
• ISSNs: 0044-2313

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Nitrogenase converts gaseous dinitrogen into biologically accessible ammonia. The binding of N₂ 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. N₂ can associate to iron or molybdenum with iron being the preferred binding site. While <italic>endo</italic> and <italic>exo</italic> binding modes were investigated the <italic>exo</italic> modes are more stable. Implications on the mechanism of N₂ reduction are discussed.</p> </abstract>