Electronic structure of iron dinitrogen complex [(TPB)FeN₂]^2-/1-/0: correlation to Mossbauer parameters.

ABSTRACT: Low-valent species of iron are key intermediates in many important biological processes such as the nitrogenase enzymatic catalytic reaction. These species play a major role in activating highly stable N₂ molecules. Thus, there is a clear need to establish the factors which are responsible for the reactivity of the metal-dinitrogen moiety. In this regard, we have investigated the electronic structure of low-valent iron (2-/1-/0) in a [(TPB)FeN₂]^2-/1-/0 complex using density functional theory (DFT). The variation in the oxidation states of iron in the nitrogenase enzyme cycle is associated with the flexibility of Fe→B bonding. Therefore, the flexibility of Fe→B bonding acts as an electron source that sustains the formation of various oxidation states, which

SUBMITTER: Vyas N 

PROVIDER: S-EPMC9049905 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature