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文献和实验Protocols for Cofactor Isolation of Nitrogenase
The iron-molybdenum cofactor (FeMoco) of the nitrogenase MoFe protein has remained a focal point in the field of bioinorganic chemistry for decades. This unique metal cluster has long been regarded as the actual site of dinitrogen reduction
Modeling the MoFe Nitrogenase System with Broken Symmetry Density Functional Theory
molybdenum cofactor (FeMo-co) where N2 reduction occurs within MoFe nitrogenase is challenging. Therefore, the enhancement of DFT to include broken symmetry (BS-DFT) plus approximate spin projection has proven valuable because it provides a procedure
Methods for Nitrogenase-Like Dark Operative Protochlorophyllide Oxidoreductase
to nitrogenase catalysis, since no molybdenum-containing cofactor or a P-cluster equivalent is employed. Instead, two consecutive electron transfer steps are mediated via the [4Fe–4S] cluster of (ChlN/ChlB)2 , resulting in the reduction of the conjugated ring
