Dinitrogen Binding and Activation: Bonding Analyses of Stable V(III/I)-N₂-V(III/I) Complexes by the EDA-NOCV Method...

The FeVco cofactor of nitrogenase (VFe₇S₈(CO₃)C) is an alternative in the molybdenum (Mo)-deficient free soil living azotobacter vinelandii. The rate of N₂ reduction to NH₃ by FeVco is a few times higher than that by FeMoco (MoFe₇S₉C) at low temperature. It provides a N source in the form of ammonium ions to the soil. This biochemical NH₃ synthesis is an alternative to the industrial energy-demanding production of NH₃ by the Haber-Bosch process. The role of vanadium has not been clearly understood yet, which has led chemists to come up with several stable V-N₂ complexes which have been isolated and characterized in the laboratory over the past three decades. Herein, we report the EDA-NOCV analyses of dinitrogen-bonded stable complexes V(III/I)-N₂ (1-4) to provide deeper insights into the fundamental bonding aspects of V-N₂ bond, showing the interacting orbitals and corresponding pairwise orbital interaction energies (ΔE _orb(). The computed intrinsic interaction energy (ΔE _int) of V-N₂-V bonds is significantly higher than those of the previously reported Fe-N₂-Fe bonds. Covalent interaction energy (ΔE _orb) is more than double the electrostatic interaction energy (ΔE _elstat) of V-N₂-V bonds. ΔE _int values of V-N₂-V bonds are in the range of -172 to -204 kcal/mol. The V → N₂ ← V π-backdonation is four times stronger than V ← N₂ → V σ-donation. V-N₂ bonds are much more covalent in nature than Fe-N₂ bonds.