The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom

Abstract: The first direct evidence is provided for the presence of an interstitial carbide in the Fe-V cofactor of Azotobacter vinelandii vanadium nitrogenase. As for our identification of the central carbide in the Fe-Mo cofactor, we employed Fe Kβ valence‐to‐core X‐ray emission spectroscopy and density functional theory calculations, and herein report the highly similar spectra of both variants of the cofactor‐containing protein. The identification of an analogous carbide, and thus an atomically homologous active site in vanadium nitrogenase, highlights the importance and influence of both the interstitial carbide and the identity of the heteroatom on the electronic structure and catalytic activity of the enzyme

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch
• Notes: Angewandte Chemie / International edition. 54, 45 (2015), 13249-13252, DOI 10.1002/anie.201505930, issn: 1521-3773

Classification and Topics

• Keyword: Cofaktor ; Nitrogenase ; Vanadium ; Röntgenspektroskopie

Contributors, Places and Time

• Event: Veröffentlichung
• (where): Freiburg
• (who): Universität
• (when): 2018
• Creator: Rees, Julian A. ; Bjornsson, Ragnar ; Netzer, Julia Clarissa ; Sippel, Daniel ; Einsle, Oliver ; DeBeer, Serena
• Contributor: Albert-Ludwigs-Universität Freiburg. Institut für Biochemie ; Albert-Ludwigs-Universität Freiburg. Centre for Biological Signalling Studies ; Albert-Ludwigs-Universität Freiburg

Further information

• DOI: 10.1002/anie.201505930
• URN: urn:nbn:de:bsz:25-freidok-150522
• Rights: Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 25.03.2025, 1:49 PM CET