Abstract
The molybdenum atom in FeMoco is imperative to the high activity of the enzyme and has been proposed to be Mo(iv). We demonstrate that only Mo(iii) fits Mo HERFD XAS data, the first example of Mo(iii) in biology. Theoretical calculations further reveal an unusual spin-coupled Mo(iii).
Highlights
Nitrogenase is the enzyme responsible for the catalytic reduction of dinitrogen (N2) to ammonia
We show that the detailed comparison of protein and model Mo-HERFD XAS data together with the results of density functional theory (DFT) calculations requires a revised oxidation state assignment for molybdenum in the resting state of FeMo cofactor (FeMoco)
As the only Mo present in the MoFe protein is associated with FeMoco, the spectrum corresponds to a unique Mo site
Summary
Nitrogenase is the enzyme responsible for the catalytic reduction of dinitrogen (N2) to ammonia. We show that the detailed comparison of protein and model Mo-HERFD XAS data together with the results of density functional theory (DFT) calculations requires a revised oxidation state assignment for molybdenum in the resting state of FeMoco.
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