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  Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms

Nikolaev, A., Safarian, S., Thesseling, A., Wohlwend, D., Friedrich, T., Michel, H., et al. (2021). Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms. Biochimica et Biophysica Acta, Bioenergetics, 1862(8): e148436. doi:10.1016/j.bbabio.2021.148436.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0008-7022-3 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0008-80BF-0
Genre: Zeitschriftenartikel

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 Urheber:
Nikolaev, Anton1, Autor
Safarian, Schara2, Autor           
Thesseling, Alexander3, Autor
Wohlwend, Daniel3, Autor
Friedrich, Thorsten3, Autor
Michel, Hartmut2, Autor           
Kusumoto, Tomoichirou4, Autor
Sakamoto, Junshi4, Autor
Melin, Frederic1, Autor
Hellwig, Petra1, 5, Autor
Affiliations:
1Laboratoire de Bioélectrochimie et Spectroscopie, UMR 7140, Chimie de la Matière Complexe, Université de Strasbourg – CNRS 4, rue Blaise Pascal, 67081 Strasborg, France, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany, ou_persistent22              
4Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, 680-4 Kawazu, Fukuoka, Japan, ou_persistent22              
5USIAS, University of Strasbourg Institute for Advanced Studies, Strasbourg, France, ou_persistent22              

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Schlagwörter: cytochrome bd oxidase; electrocatalysis; oxygen reduction; diversity of enzymatic reactions; bacterial adaptation
 Zusammenfassung: Cytochrome bd oxidase is a bacterial terminal oxygen reductase that was suggested to enable adaptation to different environments and to confer resistance to stress conditions. An electrocatalytic study of the cyt bd oxidases from Escherichia coli, Corynebacterium glutamicum and Geobacillus thermodenitrificans gives evidence for a different reactivity towards oxygen. An inversion of the redox potential values of the three hemes is found when comparing the enzymes from different bacteria. This inversion can be correlated with different protonated glutamic acids as evidenced by reaction induced FTIR spectroscopy. The influence of the microenvironment of the hemes on the reactivity towards oxygen is discussed.

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Sprache(n): eng - English
 Datum: 2021-04-162020-12-032021-04-212021-04-30
 Publikationsstatus: Online veröffentlicht
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/j.bbabio.2021.148436
PMID: 33940039
 Art des Abschluß: -

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Titel: Biochimica et Biophysica Acta, Bioenergetics
  Kurztitel : Biochim. Biophys. Acta, Bioenerg.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 1862 (8) Artikelnummer: e148436 Start- / Endseite: - Identifikator: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6