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
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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Science Advances. - 7, 22 (2021) , abg4474, ISSN: 2375-2548
- Klassifikation
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Biowissenschaften, Biologie
- Ereignis
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Veröffentlichung
- (wo)
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Freiburg
- (wer)
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Universität
- (wann)
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2023
- Urheber
- Beteiligte Personen und Organisationen
- DOI
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10.1126/sciadv.abg4474
- URN
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urn:nbn:de:bsz:25-freidok-2363930
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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25.03.2025, 13:56 MEZ
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Beteiligte
- Rohde, Michael
- Laun, Konstantin
- Zebger, Ingo
- Stripp, Sven T.
- Einsle, Oliver
- Albert-Ludwigs-Universität Freiburg. Institut für Biochemie
- Universität
Entstanden
- 2023
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