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  Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans

von der Hocht, I., van Wonderen, J. H., Hilbers, F., Angerer, H., MacMillan, F., & Michel, H. (2011). Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans. Proceedings of the National Academy of Sciences of the United States of America, 108(10), 3964-3969. doi:10.1073/pnas.1100950108.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D5F8-9 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0007-11D1-9
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 Urheber:
von der Hocht, Iris1, Autor           
van Wonderen, Jessica H.2, Autor
Hilbers, Florian1, Autor           
Angerer, Heike1, Autor           
MacMillan, Fraser2, Autor
Michel, Hartmut1, Autor           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Henry Wellcome Unit for BiologicalElectron Paramagnetic Resonance Spectroscopy, School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom, ou_persistent22              

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Schlagwörter: artificial intermediates; catalase activity; electron paramagnetic resonance spectroscopy; optical difference spectroscopy
 Zusammenfassung: Cytochrome c oxidase (CcO) is the terminal enzyme of the respiratory chain. This redox-driven proton pump catalyzes the fourelectron reduction of molecular oxygen to water, one of the most fundamental processes in biology. Elucidation of the intermediate structures in the catalytic cycle is crucial for understanding both the mechanism of oxygen reduction and its coupling to proton pumping. Using CcO from Paracoccus denitrificans, we demonstrate that the artificial F state, classically generated by reaction with an excess of hydrogen peroxide, can be converted into a new P state (in contradiction to the conventional direction of the catalytic cycle) by addition of ammonia at pH 9. We suggest that ammonia coordinates directly to CuB in the binuclear active center in this P state and discuss the chemical structures of both oxoferryl intermediates F and P. Our results are compatible with a superoxide bound to CuB in the F state.

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Sprache(n): eng - English
 Datum: 2011-03-08
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.1100950108
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Andere : Proceedings of the National Academy of Sciences of the USA
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 108 (10) Artikelnummer: - Start- / Endseite: 3964 - 3969 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230