Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  A nitric oxide-binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase

Akram, M., Reimann, J., Dietl, A., Menzel, A., Versantvoort, W., Kartal, B., et al. (2019). A nitric oxide-binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase. The Journal of Biological Chemistry, e-pup(788), 1-29. doi:10.1074/jbc.RA119.008788.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel

Dateien

einblenden: Dateien
ausblenden: Dateien
:
JBiolChem_e-pup_2019_788.pdf (beliebiger Volltext), 3MB
 
Datei-Permalink:
-
Name:
JBiolChem_e-pup_2019_788.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Eingeschränkt (Max Planck Institute for Medical Research, MHMF; )
MIME-Typ / Prüfsumme:
application/pdf
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:
ausblenden:
Beschreibung:
-
OA-Status:
externe Referenz:
https://doi.org/10.1074/jbc.RA119.008788 (beliebiger Volltext)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Akram, Mohd1, 2, 3, Autor           
Reimann, Joachim, Autor
Dietl, Andreas1, 3, 4, 5, Autor           
Menzel, Andreas, Autor
Versantvoort, Wouter, Autor
Kartal, Boran, Autor
Jetten, Mike S.M., Autor
Barends, Thomas1, 2, 3, 4, 5, 6, Autor           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
3Structural Biology of Elemental Cycles, Max Planck Institute for Medical Research, Max Planck Society, ou_2205646              
4Heme and Flavin Enzymes, Max Planck Institute for Medical Research, Max Planck Society, ou_1497715              
5Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              
6Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              

Inhalt

einblenden:
ausblenden:
Schlagwörter: cytochrome c, nitric oxide, redox, bacterial metabolism, crystal structure, UV-Vis spectroscopy, anaerobic ammonium oxidation (anammox), NaxLS, nitrogen cycle, electron transport
 Zusammenfassung: Anaerobic ammonium oxidation (anammox) is a microbial process responsible for significant nitrogen loss from the oceans and other ecosystems. The redox reactions at the heart of anammox are catalyzed by large multiheme enzyme complexes that rely on small cytochrome c proteins for electron shuttling. Among the most highly abundant of these cytochromes is a unique heterodimeric complex composed of class I and class II c-type cytochrome called NaxLS, which has distinctive biochemical and spectroscopic properties. Here, we present the 1.7 Å resolution crystal structure of this complex from the anammox organism Kuenenia stuttgartiensis (KsNaxLS). The structure reveals that the heme irons in each subunit exhibit a rare His/Cys ligation, which, as we show by substitution, causes the observed unusual spectral properties. Unlike its individual subunits, the KsNaxLS complex binds nitric oxide (NO) only at the distal heme side, forming 6cNO adducts. This is likely due to steric immobilization of the proximal heme binding motifs upon complex formation, a finding that may be of functional relevance, since NO is an intermediate in the central anammox metabolism. Pulldown experiments with K. stuttgartiensis cell-free extract showed that the KsNaxLS complex binds specifically to one of the central anammox enzyme complexes, hydrazine synthase, which uses NO as one of its substrates. It is therefore possible that the KsNaxLS complex plays a role in binding the volatile NO to retain it in the cell for transfer to hydrazine synthase. Alternatively, we propose that KsNaxLS may shuttle electrons to this enzyme complex.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2019-09-22
 Publikationsstatus: Erschienen
 Seiten: 29
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1074/jbc.RA119.008788
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: The Journal of Biological Chemistry
  Andere : JBC
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: e-pup (788) Artikelnummer: - Start- / Endseite: 1 - 29 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1