Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
Abstract: Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C2H4), implying a C–C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 Å resolution, with one μ-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion
- 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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Science Advances. - 7, 22 (2021) , abg4474, ISSN: 2375-2548
- Classification
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Biowissenschaften, Biologie
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2023
- Creator
- DOI
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10.1126/sciadv.abg4474
- URN
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urn:nbn:de:bsz:25-freidok-2363930
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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25.03.2025, 1:56 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Rohde, Michael
- Laun, Konstantin
- Zebger, Ingo
- Stripp, Sven T.
- Einsle, Oliver
- Albert-Ludwigs-Universität Freiburg. Institut für Biochemie
- Universität
Time of origin
- 2023
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Investigation of carbon monoxide binding to vanadium nitrogenase
CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
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Structure and function of cytochrome c nitrite reductase
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
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
CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
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
The Iron-only nitrogenase system of Azotobacter vinelandii
Structural analysis of the reductase component AnfH of iron-only nitrogenase from Azotobacter vinelandii
Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
On the shoulders of giants - reaching for nitrogenase
Structure and function of cytochrome c nitrite reductase
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
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
CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
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
The Iron-only nitrogenase system of Azotobacter vinelandii
Structural analysis of the reductase component AnfH of iron-only nitrogenase from Azotobacter vinelandii
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