Activation and Protonation of Dinitrogen at the FeMo-Cofactor of Nitrogenase

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dc.creatorKaestner, Johannes
dc.creatorHemmen, Sascha
dc.creatorBloechl, Peter E.
dc.date2005-07-08
dc.date2005-08-23
dc.date.accessioned2026-07-07T05:59:21Z
dc.date.available2026-07-07T05:59:21Z
dc.descriptionThe protonation of N2 bound to the active center of nitrogenase has been investigated using state-of-the-art DFT calculations. Dinitrogen in the bridging mode is activated by forming two bonds to Fe sites, which results in a reduction of the energy for the first hydrogen transfer by 123 kJ/mol. The axial binding mode with open sulfur bridge is less reactive by 30 kJ/mol and the energetic ordering of the axial and bridged binding mode is reversed in favor of the bridging dinitrogen during the first protonation. Protonation of the central ligand is thermodynamically favorable but kinetically hindered. If the central ligand is protonated, the proton is transferred to dinitrogen following the second protonation. Protonation of dinitrogen at the Mo site does not lead to low-energy intermediates.
dc.description9 Pages, 6 figures, accepted in J. Chem. Phys. Typos corrected according to the galley proofs of JCP
dc.identifierhttps://arxiv.org/abs/q-bio/0507012
dc.identifierhttp://arxiv.org/abs/q-bio/0507012
dc.identifierJ. Chem. Phys. 123, 074306 (2005)
dc.identifierdoi:10.1063/1.2008227
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88650
dc.subjectBiomolecules
dc.titleActivation and Protonation of Dinitrogen at the FeMo-Cofactor of Nitrogenase
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