Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

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

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch
Notes
Nature communications. 7 (2016), article no. 10902, DOI 10.1038/ncomms10902, issn: 2041-1723

Keyword
Nitrogenase
Anomale Dispersion
Biogeochemie
Metalloproteinasen
Oxidoreductasen
Strukturbiologie

Event
Veröffentlichung
(where)
Freiburg
(who)
Universität
(when)
2018
Creator
Contributor

DOI
10.1038/ncomms10902
URN
urn:nbn:de:bsz:25-freidok-150424
Rights
Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
14.08.2025, 10:49 AM CEST

Data provider

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Time of origin

  • 2018

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