Comparative electronic structures of nitrogenase FeMoco and FeVco
Abstract: An investigation of the active site cofactors of the molybdenum and vanadium nitrogenases (FeMoco and FeVco) was performed using high-resolution X-ray spectroscopy. Synthetic heterometallic iron–sulfur cluster models and density functional theory calculations complement the study of the MoFe and VFe holoproteins using both non-resonant and resonant X-ray emission spectroscopy. Spectroscopic data show the presence of direct iron–heterometal bonds, which are found to be weaker in FeVco. Furthermore, the interstitial carbide is found to perturb the electronic structures of the cofactors through highly covalent Fe–C bonding. The implications of these conclusions are discussed in light of the differential reactivity of the molybdenum and vanadium nitrogenases towards various substrates. Possible functional roles for both the heterometal and the interstitial carbide are detailed
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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Dalton transactions. 46, 8 (2017), 2445-2455, DOI 10.1039/c7dt00128b, issn: 1477-9234
- Keyword
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Vanadiumnitride
Nitrogenase
Elektronenstruktur
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2018
- Creator
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Rees, Julian A.
Bjornsson, Ragnar
Kowalska, Joanna K.
Lima, Frederico A.
Netzer, Julia Clarissa
Sippel, Daniel
Weyhermüller, Thomas
Einsle, Oliver
Kovacs, Julie A.
DeBeer, Serena
- DOI
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10.1039/c7dt00128b
- URN
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urn:nbn:de:bsz:25-freidok-150312
- Rights
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Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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25.03.2025, 1:49 PM CET
Data provider
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Associated
- Rees, Julian A.
- Bjornsson, Ragnar
- Kowalska, Joanna K.
- Lima, Frederico A.
- Netzer, Julia Clarissa
- Sippel, Daniel
- Weyhermüller, Thomas
- Einsle, Oliver
- Kovacs, Julie A.
- DeBeer, Serena
- Albert-Ludwigs-Universität Freiburg. Institut für Biochemie
- Albert-Ludwigs-Universität Freiburg. Centre for Biological Signalling Studies
- Albert-Ludwigs-Universität Freiburg
- Universität
Time of origin
- 2018
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Structure and function of cytochrome c nitrite reductase
Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Structural characterisation of nitrogen fixation by the enzyme nitrogenase of Azotobacter vinelandii
Investigation of carbon monoxide binding to vanadium nitrogenase
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On the shoulders of giants - reaching for nitrogenase
Structural, electronic and magnetic characterization of the nitrogenase active site FeMo-cofactor and crystallization of the ketol-acid reductoisomerase from Azotobacter vinelandii : = Strukturelle, elektronische und magnetische Charakterisierung des Aktivzentrums der Nitrogenase (FeMo-Kofaktor) und Kristallisation der Acetohydroxysäure-Reduktoisomerase aus Azotobacter vinelandii
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Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
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Investigation of carbon monoxide binding to vanadium nitrogenase
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