CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
Abstract: Nitrogenases reduce N2, the most abundant element in Earth's atmosphere that is otherwise resistant to chemical conversions due to its stable triple bond. Vanadium nitrogenase stands out in that it additionally processes carbon monoxide, a known inhibitor of the reduction of all substrates other than H+. The reduction of CO leads to the formation of hydrocarbon products, holding the potential for biotechnological applications in analogy to the industrial Fischer–Tropsch process. Here we report the most highly resolved structure of vanadium nitrogenase to date at 1.0 Å resolution, with CO bound to the active site cofactor after catalytic turnover. CO bridges iron ions Fe2 and Fe6, replacing sulfide S2B, in a binding mode that is in line with previous reports on the CO complex of molybdenum nitrogenase. We discuss the structural consequences of continued turnover when CO is removed, which involve the replacement of CO possibly by OH−, the movement of Q176D and K361D, the return of sulfide and the emergence of two additional water molecules that are absent in the CO‐bound state
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Angewandte Chemie. International edition. - 59, 52 (2020) , 23626-23630, ISSN: 1521-3773
- Ereignis
-
Veröffentlichung
- (wo)
-
Freiburg
- (wer)
-
Universität
- (wann)
-
2021
- DOI
-
10.1002/anie.202010790
- URN
-
urn:nbn:de:bsz:25-freidok-1752173
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:56 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Rohde, Michael
- Grunau, Katharina
- Einsle, Oliver
- Universität
Entstanden
- 2021
Ähnliche Objekte (12)
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
On the shoulders of giants - reaching for nitrogenase
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
Structure and function of cytochrome c nitrite reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Structural characterisation of nitrogen fixation by the enzyme nitrogenase of Azotobacter vinelandii
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
Investigation of carbon monoxide binding to vanadium nitrogenase
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
Identification of a spin-coupled Mo(III) in the nitrogenase iron-molybdenum cofactor
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
On the shoulders of giants - reaching for nitrogenase
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
Structure and function of cytochrome c nitrite reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Structural characterisation of nitrogen fixation by the enzyme nitrogenase of Azotobacter vinelandii
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
Investigation of carbon monoxide binding to vanadium nitrogenase
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
Identification of a spin-coupled Mo(III) in the nitrogenase iron-molybdenum cofactor
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
On the shoulders of giants - reaching for nitrogenase
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
Structure and function of cytochrome c nitrite reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Structural characterisation of nitrogen fixation by the enzyme nitrogenase of Azotobacter vinelandii
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
Investigation of carbon monoxide binding to vanadium nitrogenase
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle