Oxidatively Induced Reductive N₂ Binding: A Dinickel-Bridging Bent N₂ Radical Anion and Its Redox-Triggered N₂ Release.

ABSTRACT: Nitrogenase accumulates reducing equivalents in hydrides and couples H₂ elimination to the reductive binding of N₂ at a di-iron edge of its FeMo cofactor (FeMoco). Here, we describe that oxidation of a pyrazolato-based dinickel(II) dihydride complex K[L(Ni-H)₂] (1^K), either electrochemically or chemically using H⁺ or ferrocenium, triggers H₂ elimination and binding of N₂ in a constrained and extremely bent bridging mode in [LNi₂(μ_1,2-N₂)] (3^N2). Spectroscopic and computational evidence indicate that the electronic structure of 3^N2 is best described as Ni^II-(N₂^•-)-Ni^II, with a

SUBMITTER: Mozzi SI 

PROVIDER: S-EPMC12447506 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature