Identification of a spin-coupled Mo(III) in the nitrogenase iron-molybdenum cofactor
Abstract: Nitrogenase is the enzyme responsible for the catalytic reduction of dinitrogen (N2) to ammonia. In contrast to the industrial Haber–Bosch process that reacts N2 and H2 at high temperature and pressure, the biological reduction proceeds at ambient temperature and pressure using a complex multicomponent protein system, which utilizes eight electrons, eight protons and 16 MgATP molecules.1,2 Unraveling the structural and mechanistic details of how nature activates the strong bond of dinitrogen is of fundamental importance and this knowledge could aid in the design of better catalysts
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Chemical science. 5, 8 (2014), 3096-3103, DOI 10.1039/c4sc00337c, issn: 2041-6539
- Keyword
-
Nitrogenase
Haber-Bosch-Verfahren
Katalyse
Anorganische Chemie
- Event
-
Veröffentlichung
- (where)
-
Freiburg
- (who)
-
Universität
- (when)
-
2018
- Creator
-
Bjornsson, Ragnar
Lima, Frederico A.
Spatzal, Thomas
Weyhermüller, Thomas
Glatzel, Pieter
Bill, Eckhard
Einsle, Oliver
Neese, Frank
DeBeer, Serena
- Contributor
- DOI
-
10.1039/c4sc00337c
- URN
-
urn:nbn:de:bsz:25-freidok-150634
- Rights
-
Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 14.08.2025, 11:02 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
- Bjornsson, Ragnar
- Lima, Frederico A.
- Spatzal, Thomas
- Weyhermüller, Thomas
- Glatzel, Pieter
- Bill, Eckhard
- Einsle, Oliver
- Neese, Frank
- DeBeer, Serena
- Albert-Ludwigs-Universität Freiburg. Institut für Biochemie
- Albert-Ludwigs-Universität Freiburg
- Universität
Time of origin
- 2018
Other Objects (12)
CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
On the shoulders of giants - reaching for nitrogenase
CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
Structure and function of cytochrome c nitrite reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
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
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
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
X‐ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin‐Coupled Molybdenum (III) Center
CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
On the shoulders of giants - reaching for nitrogenase
CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
Structure and function of cytochrome c nitrite reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
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
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
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom
X‐ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin‐Coupled Molybdenum (III) Center
CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
On the shoulders of giants - reaching for nitrogenase
CO binding to the FeV cofactor of CO‐reducing vanadium nitrogenase at atomic resolution
Structure and function of cytochrome c nitrite reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Investigation of complex formation and the FeV cofactor of Vanadium Nitrogenase
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
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
The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom