Wavelength dependent photochemistry of an iron dinitrogen hydride complex <i>via</i> multiple spectroscopies - competing ejection of axial ligands.

ABSTRACT: Nitrogenase (N₂ase) is a critical enzyme which catalyzes the reaction of N₂ → NH₃ in nature. Studies on the spectroscopy and photochemistry of trans-[Fe^II(DMeOPrPE)₂(N₂)H][BPh₄] (1) and its isotopologues (2-6) provide a possible first step to evaluate the geometries and properties of the real N₂ase-N₂ structure(s). In this article, we have used FT-IR, FT-Raman, synchrotron-based nuclear resonant vibrational spectroscopy (NRVS) and DFT calculations to examine and assign the normal modes of these complexes. In addition, we have monitored their wavelength dependent photochemistry using mid-IR, near-IR, NRVS, and Mössbauer spectroscopies. Two distinct photolysis pathways are observed with

SUBMITTER: Dong W 

PROVIDER: S-EPMC12268277 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature