Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

Thomas Spatzal, Julia Schlesier, Eva Maria Burger, Daniel Sippel, Limei Zhang, Susana L.A. Andrade, Douglas C. Rees, Oliver Einsle

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catalyses the 6-electron reduction of dinitrogen to ammonium in biological nitrogen fixation. Only recently its atomic structure was clarified, while its reactivity and electronic structure remain under debate. Here we show that for its resting S=3/2 state the common iron oxidation state assignments must be reconsidered. By a spatially resolved refinement of the anomalous scattering contributions of the 7 Fe atoms of FeMoco, we conclude that three irons (Fe1/3/7) are more reduced than the other four (Fe2/4/5/6). Our data are in agreement with the recently revised oxidation state assignment for the molybdenum ion, providing the first spatially resolved picture of the resting-state electron distribution within FeMoco. This might provide the long-sought experimental basis for a generally accepted theoretical description of the cluster that is in line with available spectroscopic and functional data.

Original languageEnglish (US)
JournalNature communications
Volume7
DOIs
StatePublished - Mar 14 2016

Fingerprint

State assignment
Nitrogenase
Molybdoferredoxin
Electrons
Nitrogen fixation
Crystal atomic structure
iron
Oxidation
Nitrogen Fixation
molybdenum
Molybdenum
Ammonium Compounds
Electron energy levels
nitrogenation
Electronic structure
oxidation
Iron
Metals
metal clusters
Scattering

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Spatzal, T., Schlesier, J., Burger, E. M., Sippel, D., Zhang, L., Andrade, S. L. A., ... Einsle, O. (2016). Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement. Nature communications, 7. https://doi.org/10.1038/ncomms10902

Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement. / Spatzal, Thomas; Schlesier, Julia; Burger, Eva Maria; Sippel, Daniel; Zhang, Limei; Andrade, Susana L.A.; Rees, Douglas C.; Einsle, Oliver.

In: Nature communications, Vol. 7, 14.03.2016.

Research output: Contribution to journalArticle

Spatzal, T, Schlesier, J, Burger, EM, Sippel, D, Zhang, L, Andrade, SLA, Rees, DC & Einsle, O 2016, 'Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement', Nature communications, vol. 7. https://doi.org/10.1038/ncomms10902
Spatzal, Thomas ; Schlesier, Julia ; Burger, Eva Maria ; Sippel, Daniel ; Zhang, Limei ; Andrade, Susana L.A. ; Rees, Douglas C. ; Einsle, Oliver. / Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement. In: Nature communications. 2016 ; Vol. 7.
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AU - Rees, Douglas C.

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