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

ABSTRACT: 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 E

SUBMITTER: Chauhan A

PROVIDER: S-EPMC9453968 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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Dataset Information

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

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Dataset Information

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

OmicsDI is part of the ELIXIR infrastructure

Tweets

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