Electronic Spectra of Iron-Sulfur Complexes Measured by 2p3d RIXS Spectroscopy

Inorganic Chemistry
Benjamin E Van KuikenSerena DeBeer

Abstract

Iron sulfur (FeS) proteins perform a wide range of biological functions including electron transfer and catalysis. Understanding the complex reactivity of these systems requires a detailed understanding of their electronic properties, which are encoded in the low-energy d-d excited states. Here we demonstrate that iron L-edge 2p3d resonant inelastic X-ray scattering (RIXS) can measure d-d excitation spectra in a series of monomeric, dimeric, and tetrameric FeS model complexes. RIXS provides advantages over traditional optical spectroscopies, because it is capable of measuring low-energy electronic excitations (0-10 000 cm-1) and spin-flip transitions. RIXS reveals the dense manifold of d-d excited states in dimeric [2Fe-2S] and tetrameric [MFe3S4]2+ (M = V or Mo) complexes resulting from covalency and exchange coupling. These results support recent ab initio theoretical predictions that FeS clusters possess a much greater number of low-lying excited states than predicted by model Hamiltonians.

References

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May 11, 2018·Methods in Enzymology·Sven-Andreas FreibertRoland Lill

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Citations

Apr 2, 2019·Philosophical Transactions. Series A, Mathematical, Physical, and Engineering Sciences·Nina Rohringer

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