On the shoulders of giants - reaching for nitrogenase
Abstract: Only a single enzyme system—nitrogenase—carries out the conversion of atmospheric N2 into bioavailable ammonium, an essential prerequisite for all organismic life. The reduction of this inert substrate at ambient conditions poses unique catalytic challenges that strain our mechanistic understanding even after decades of intense research. Structural biology has added its part to this greater tapestry, and in this review, I provide a personal (and highly biased) summary of the parts of the story to which I had the privilege to contribute. It focuses on the crystallographic analysis of the three isoforms of nitrogenases at high resolution and the binding of ligands and inhibitors to the active-site cofactors of the enzyme. In conjunction with the wealth of available biochemical, biophysical, and spectroscopic data on the protein, this has led us to a mechanistic hypothesis based on an elementary mechanism of repetitive hydride formation and insertion
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Molecules. - 28, 24 (2023) , 7959, ISSN: 1420-3049
- DOI
-
10.3390/molecules28247959
- URN
-
urn:nbn:de:bsz:25-freidok-2419071
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:30 AM CEST
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
- Einsle, Oliver
- Universität
Time of origin
- 2023
Other Objects (12)
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
Bindung von CO am FeV‐Cofaktor der CO‐reduzierenden Vanadium‐Nitrogenase bei atomarer Auflösung
CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
Investigation of carbon monoxide binding to vanadium nitrogenase
Bindung von CO am FeV‐Cofaktor der CO‐reduzierenden Vanadium‐Nitrogenase bei atomarer Auflösung
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
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
Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase
The Iron-only nitrogenase system of Azotobacter vinelandii
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
Bindung von CO am FeV‐Cofaktor der CO‐reduzierenden Vanadium‐Nitrogenase bei atomarer Auflösung
CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
Investigation of carbon monoxide binding to vanadium nitrogenase
Bindung von CO am FeV‐Cofaktor der CO‐reduzierenden Vanadium‐Nitrogenase bei atomarer Auflösung
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
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
Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase
The Iron-only nitrogenase system of Azotobacter vinelandii
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
Bindung von CO am FeV‐Cofaktor der CO‐reduzierenden Vanadium‐Nitrogenase bei atomarer Auflösung
CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
Investigation of carbon monoxide binding to vanadium nitrogenase
Bindung von CO am FeV‐Cofaktor der CO‐reduzierenden Vanadium‐Nitrogenase bei atomarer Auflösung
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation
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
Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase