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X-ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin-Coupled Molybdenum(III) Center

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Kowalska,  Joanna K.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Henthorn,  Justin Travis
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Van Stappen,  Casey
IMPRS-RECHARGE, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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DeBeer,  Serena
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Kowalska, J. K., Henthorn, J. T., Van Stappen, C., Trncik, C., Einsle, O., Keavney, D., et al. (2019). X-ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin-Coupled Molybdenum(III) Center. Angewandte Chemie, International Edition in English, 58(28), 9373-9377. doi:10.1002/anie.201901899.


Cite as: https://hdl.handle.net/21.11116/0000-0006-4037-4
Abstract
Nitrogenase enzymes catalyze the reduction of atmospheric dinitrogen to ammonia utilizing a Mo-7Fe-9S-C active site, the so-called FeMoco cluster. FeMoco and an analogous small-molecule (Et4N)[(Tp)MoFe3S4Cl3] cubane have both been proposed to contain unusual spin-coupled Mo-III sites with an S(Mo)=1/2 non-Hund configuration at the Mo atom. Herein, we present Fe and Mo L-3-edge X-ray magnetic circular dichroism (XMCD) spectroscopy of the (Et4N)[(Tp)MoFe3S4Cl3] cubane and Fe L-2,L-3-edge XMCD spectroscopy of the MoFe protein (containing both FeMoco and the 8Fe-7S P-cluster active sites). As the P-clusters of MoFe protein have an S=0 total spin, these are effectively XMCD-silent at low temperature and high magnetic field, allowing for FeMoco to be selectively probed by Fe L-2,L-3-edge XMCD within the intact MoFe protein. Further, Mo L-3-edge XMCD spectroscopy of the cubane model has provided experimental support for a local S(Mo)=1/2 configuration, demonstrating the power and selectivity of XMCD.