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Naji, M. |
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Motta, Antonella |
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Aletan, Dirar |
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Mohamed, Tarek |
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Ertürk, Emre |
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Taccardi, Nicola |
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Kononenko, Denys |
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Petrov, R. H. | Madrid |
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Alshaaer, Mazen | Brussels |
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Bih, L. |
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Casati, R. |
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Muller, Hermance |
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Kočí, Jan | Prague |
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Šuljagić, Marija |
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Kalteremidou, Kalliopi-Artemi | Brussels |
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Azam, Siraj |
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Ospanova, Alyiya |
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Blanpain, Bart |
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Ali, M. A. |
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Popa, V. |
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Rančić, M. |
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Ollier, Nadège |
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Azevedo, Nuno Monteiro |
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Landes, Michael |
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Rignanese, Gian-Marco |
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Debeer, Serena
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (10/10 displayed)
- 2024Highly loaded bimetallic iron-cobalt catalysts for hydrogen release from ammoniacitations
- 2024Probing the Local Environment in Potassium Salts and Potassium-Promoted Catalysts by Potassium Valence-to-Core X-ray Emission Spectroscopycitations
- 2023Structural correlations of nitrogenase active sites using nuclear resonance vibrational spectroscopy and QM/MM calculationscitations
- 2022Determination of the iron(IV) local spin states of the Q intermediate of soluble methane monooxygenase by Kβ X-ray emission spectroscopy.citations
- 20223D atomic-scale imaging of mixed Co-Fe spinel oxide nanoparticles during oxygen evolution reaction
- 2022An Fe6C Core in All Nitrogenase Cofactorscitations
- 2020Ruthenium 4d-to-2p X-ray Emission Spectroscopy: A Simultaneous Probe of the Metal and the Bound Ligandscitations
- 2020Kβ X‐Ray Emission Spectroscopic Study of a Second‐Row Transition Metal (Mo) and Its Application to Nitrogenase‐Related Model Complexescitations
- 2013Experimental and computational X-ray emission spectroscopy as a direct probe of protonation states in oxo-bridged MnIV dimers relevant to redox-active metalloproteinscitations
- 2013The protonation states of oxo-bridged MnIV dimers resolved by experimental and computational Mn K pre-edge X-ray absorption spectroscopycitations
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article
An Fe6C Core in All Nitrogenase Cofactors
Abstract
<jats:title>Abstract</jats:title><jats:p>The biological process of dinitrogen reduction to ammonium occurs at the cofactors of nitrogenases, the only enzymes that catalyze this challenging chemical reaction. Three types of nitrogenases have been described, named according to the heterometal in their cofactor: molybdenum, vanadium or iron nitrogenases. Spectroscopic and structural characterization allowed the unambiguous identification of the cofactors of molybdenum and vanadium nitrogenases and revealed a central μ<jats:sub>6</jats:sub>‐carbide in both of them. Although genetic studies suggested that the cofactor of the iron nitrogenase contains a similar Fe<jats:sub>6</jats:sub>C core, this has not been experimentally demonstrated. Here we report Valence‐to‐Core X‐ray Emission Spectroscopy providing experimental evidence that this cofactor contains a carbide, thereby making the Fe<jats:sub>6</jats:sub>C core a feature of all nitrogenase cofactors.</jats:p>