Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

The Spectroscopy of Nitrogenases

MPG-Autoren
/persons/resource/persons237869

Van Stappen,  Casey
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons247915

Decamps,  Laure Benedicte
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237776

Cutsail III,  George E.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237766

Bjornsson,  Ragnar
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons246022

Henthorn,  Justin Travis
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237765

Birrell,  James A.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237560

DeBeer,  Serena
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Van Stappen, C., Decamps, L. B., Cutsail III, G. E., Bjornsson, R., Henthorn, J. T., Birrell, J. A., et al. (2020). The Spectroscopy of Nitrogenases. Chemical Reviews, 120(12), 5005-5081. doi:10.1021/acs.chemrev.9b00650.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-D4FE-C
Zusammenfassung
Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and a series of iron-sulfur clusters to perform this reaction, culminating at the FeMco active site (M = Mo, V, Fe), which is capable of binding and reducing N-2 to 2NH(3). In this review, we summarize how different spectroscopic approaches have shed light on various aspects of these enzymes, including their structure, mechanism, alternative reactivity, and maturation. Synthetic model chemistry and theory have also played significant roles in developing our present understanding of these systems and are discussed in the context of their contributions to interpreting the nature of nitrogenases. Despite years of significant progress, there is still much to be learned from these enzymes through spectroscopic means, and we highlight where further spectroscopic investigations are needed.