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Molybdenum L‐Edge XAS Spectra of MoFe Nitrogenase
Author(s) -
Bjornsson Ragnar,
DelgadoJaime Mario U.,
Lima Frederico A.,
Sippel Daniel,
Schlesier Julia,
Weyhermüller Thomas,
Einsle Oliver,
Neese Frank,
DeBeer Serena
Publication year - 2015
Publication title -
zeitschrift für anorganische und allgemeine chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.354
H-Index - 66
eISSN - 1521-3749
pISSN - 0044-2313
DOI - 10.1002/zaac.201400446
Subject(s) - x ray absorption spectroscopy , molybdenum , nitrogenase , context (archaeology) , chemistry , density functional theory , spectral line , absorption spectroscopy , spectroscopy , crystallography , physics , computational chemistry , inorganic chemistry , biology , optics , quantum mechanics , organic chemistry , paleontology , nitrogen fixation , nitrogen
A molybdenum L‐edge X‐ray absorption spectroscopy (XAS) study is presented for native and oxidized MoFe protein of nitrogenase as well as Mo‐Fe model compounds. Recently collected data on MoFe protein (in oxidized and reduced forms) is compared to previously published Mo XAS data on the isolated FeMo cofactor in NMF solution and put in context of the recent Mo K‐edge XAS study, which showed a Mo III assignment for the molybdenum atom in FeMoco. The L 3 ‐edge data are interpreted within a simple ligand‐field model, from which a time‐dependent density functional theory (TDDFT) approach is proposed as a way to provide further insights into the analysis of the molybdenum L 3 ‐edges. The calculated results reproduce well the relative spectral trends that are observed experimentally. Ultimately, these results give further support for the Mo III assignment in protein‐bound FeMoco, as well as isolated FeMoco.