Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Bound water in the proton translocation mechanism of the haem-copper oxidases

Riistama, S., Hummer, G., Puustinen, A., Brian Dyer, R., Woodruff, W. H., & Wikström, M. (1997). Bound water in the proton translocation mechanism of the haem-copper oxidases. FEBS Letters, 414(2), 275-280. doi:10.1016/S0014-5793(97)01003-X.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel

Externe Referenzen

einblenden:
ausblenden:
externe Referenz:
Link (beliebiger Volltext)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Riistama, Sirpa1, Autor
Hummer, Gerhard2, Autor                 
Puustinen, Anne1, Autor
Brian Dyer, R.1, Autor
Woodruff, William H.1, Autor
Wikström, Mårten1, Autor
Affiliations:
1External Organizations, ou_persistent22              
2Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, New Mexico, USA, ou_persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: Haem-copper oxidase, Proton translocation mechanism
 Zusammenfassung: We address the molecular mechanism by which the haem-copper oxidases translocate protons. Reduction of O2 to water takes place at a haem iron-copper (CuB) centre, and protons enter from one side of the membrane through a ‘channel’ structure in the enzyme. Statistical-mechanical calculations predict bound water molecules within this channel, and mutagenesis experiments show that breaking this water structure impedes proton translocation. Hydrogen-bonded water molecules connect the channel further via a conserved glutamic acid residue to a histidine ligand of CuB. The glutamic acid side chain may have to move during proton transfer because proton translocation is abolished if it is forced to interact with a nearby lysine or arginine. Perturbing the CuB ligand structure shifts an infrared mode that may be ascribed to the OH stretch of bound water. This is sensitive to mutations of the glutamic acid, supporting its connectivity to the histidine. These results suggest key roles of bound water, the glutamic acid and the histidine copper ligand in the mechanism of proton translocation.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 1997-07-291997-06-161997-09
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/S0014-5793(97)01003-X
BibTex Citekey: riistama_bound_1997
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: FEBS Letters
  Andere : FEBS Lett.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 414 (2) Artikelnummer: - Start- / Endseite: 275 - 280 Identifikator: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501