Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

A 192-heme electron transfer network in the hydrazine dehydrogenase complex

MPG-Autoren
/persons/resource/persons117993

Akram,  Mohd
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92666

Dietl,  Andreas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons118670

Mersdorf,  Ulli
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons233019

Prinz,  Simone
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137828

Parey,  Kristian
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons92083

Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, 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

Akram, M., Dietl, A., Mersdorf, U., Prinz, S., Maalcke, W. J., Keltjens, J. T., et al. (2019). A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Science Advances, 5(4): eaav4310. doi:10.1126/sciadv.aav4310.


Zitierlink: https://hdl.handle.net/21.11116/0000-0003-7EA2-9
Zusammenfassung
Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas and water through the highly reactive intermediate hydrazine. So far, it is unknown how anammox organisms convert the toxic hydrazine into nitrogen and harvest the extremely low potential electrons (-750 mV) released in this process. We report the crystal structure and cryo electron microscopy structures of the responsible enzyme, hydrazine dehydrogenase, which is a 1.7 MDa multiprotein complex containing an extended electron transfer network of 192 heme groups spanning the entire complex. This unique molecular arrangement suggests a way in which the protein stores and releases the electrons obtained from hydrazine conversion, the final step in the globally important anammox process.