Molecular Mechanism for Nitrogen fixation: first steps

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dc.creatorSchimpl, Johannes
dc.creatorPetrilli, Helena M.
dc.creatorBloechl, Peter E.
dc.date2003-04-09
dc.date2003-05-08
dc.date.accessioned2026-07-07T05:49:02Z
dc.date.available2026-07-07T05:49:02Z
dc.descriptionN2 association to the FeMo-cofactor of nitrogenase, including the recently identified central N ligand, has been investigated using first-principles electronic structure calculations. The oxidation state of the resting state of the cofactor and its electronic structure has been identified. A single proton is added to the sulfur bridges following each electron transfer to the cofactor. During N2 association, the cofactor undergoes large rearrangements resulting in opening the central Fe-cage of the cofactor. N2 binds axially while the bond of the bridging SH group breaks. It is then able to insert between the two Fe sites in a bridged configuration.
dc.description5 pages 2 Figures
dc.identifierhttps://arxiv.org/abs/physics/0304032
dc.identifierhttp://arxiv.org/abs/physics/0304032
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/85249
dc.subjectBiological Physics
dc.subjectChemical Physics
dc.titleMolecular Mechanism for Nitrogen fixation: first steps
dc.typetext

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