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  Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus

Kannt, A., Soulimane, T., Buse, G., Becker, A., Bamberg, E., & Michel, H. (1998). Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus. FEBS Letters, 434(1-2), 17-22. doi:10.1016/s0014-5793(98)00942-9.

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Genre: Journal Article

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 Creators:
Kannt, Aimo1, Author           
Soulimane, Tewfik 2, Author
Buse, Gerhard2, Author
Becker, Anja3, Author           
Bamberg, Ernst3, Author           
Michel, Hartmut1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institut für Biochemie, Klinikum der RWTH Aachen, Pauwelstrasse 30, 52057 Aachen, Germany, ou_persistent22              
3Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: Cytochrome c oxidase; Cytochrome ba3; Proton pumping; Black lipid membrane; Thermus thermophilus
 Abstract: Several amino acid residues that have been shown to be essential for proton transfer in most cytochrome c oxidases are not conserved in the ba3-type cytochrome c oxidase from the thermophilic eubacterium Thermus thermophilus. So far, it has been unclear whether the Th. thermophilus ba3-type cytochrome c oxidase can nevertheless function as an electrogenic proton pump. In this study, we have combined charge translocation measurements on a lipid bilayer with two independent methods of proton pumping measurements to show that enzymatic turnover of the Th. thermophilus cytochrome c oxidase is indeed coupled to the generation of an electrocurrent and proton pumping across the membrane. In addition to a 'vectorial' consumption of 1.0 H+/e- for water formation, proton pumping with a stoichiometry of 0.4-0.5 H+/e- was observed. The implications of these findings for the mechanism of redox-coupled proton transfer in this unusual cytochrome c oxidase are discussed.

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Language(s): eng - English
 Dates: 1998-07-201998-09-161998-08-28
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/s0014-5793(98)00942-9
PMID: 9738443
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 434 (1-2) Sequence Number: - Start / End Page: 17 - 22 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501