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  Zn2+ binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation

Kannt, A., Ostermann, T., Müller, H., & Ruitenberg, M. (2001). Zn2+ binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation. FEBS Letters, 503(2-3), 142-146. doi:10.1016/S0014-5793(01)02719-3.

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Genre: Journal Article

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 Creators:
Kannt, Aimo1, Author           
Ostermann, Thomas1, Author           
Müller, Hannelore1, Author           
Ruitenberg, Maarten2, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: Cytochrome c oxidase; Proton pumping; Zn2+ binding; Black lipid membrane; Proton slip
 Abstract: Using a combination of stopped-flow spectrophotometric proton pumping measurements and time-resolved potential measurements on black lipid membranes, we have investigated the effect of Zn2+ ions on the proton transfer properties of Paracoccus denitrificans cytochrome c oxidase. When zinc was enclosed in the interior of cytochrome c oxidase containing liposomes, the H/e stoichiometry was found to gradually decrease with increasing Zn2+ concentration. Half-inhibition of proton pumping was observed at [Zn2+]i=75 μM corresponding to about 5–6 Zn2+ ions per oxidase molecule. In addition, there was a significant increase in the respiratory control ratio of the proteoliposomes upon incorporation of Zn2+. Time-resolved potential measurements on a black lipid membrane showed that the electrogenic phases slowed down in the presence of Zn2+ correspond to phases that have been attributed to proton uptake from the cytoplasmic side and to proton pumping. We conclude that Zn2+ ions bind close to or within the two proton transfer pathways of the bacterial cytochrome c oxidase.

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Language(s): eng - English
 Dates: 2001-07-042001-07-072001-08-142001-08-17
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0014-5793(01)02719-3
 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: 503 (2-3) Sequence Number: - Start / End Page: 142 - 146 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501