Electronic structure of the iron-molybdenum and alternative cofactors of nitrogenases: a comparison and its consequences

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Abstract

The electronic structure of idealized structural models [H3MFe3S3{μ2−S}3Fe4S3H]n with 3m (C3) symmetry for the FeMo-, FeV-, and FeFe-cofactors of the three nitrogenase systems known (2M = Mo and n = 1, 3M = V and n = 2, 4M = Fe and n = 2) has been investigated using the EHMO and SCCC-EHMO methods, respectively. On the basis of MO analysis the similarities and differences between these model clusters will be discussed. Special attention will be focused on the possible function of the heterometal center of these model clusters (Mo, V, and Fe) as well as the binding of dinitrogen to the cofactor models.

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