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  Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Meyer, T., Melin, F., Richter, O.-M., Ludwig, B., Kannt, A., Müller, H., et al. (2015). Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants. FEBS Letters, 589(5), 565-568. doi:10.1016/j.febslet.2015.01.014.

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 Creators:
Meyer, Thomas1, Author
Melin, Frédéric1, Author
Richter, Oliver-M.H. 2, Author
Ludwig, Bernd2, Author
Kannt, Aimo3, Author           
Müller, Hanne3, Author           
Michel, Hartmut3, Author           
Hellwig, Petra1, Author
Affiliations:
1Chimie de la Matière Complexe UMR 7140, Laboratoire de Bioélectrochimie et Spectroscopie, CNRS-Université de Strasbourg, 1 rue Blaise Pascal, 67070 Strasbourg, France, ou_persistent22              
2Institute of Biochemistry, Molecular Genetics, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Cytochrome c oxidase; Zn2+ inhibition; Proton pumping; Bioelectrochemistry
 Abstract: Two different pathways through which protons access cytochrome c oxidase operate during oxygen reduction from the mitochondrial matrix, or the bacterial cytoplasm. Here, we use electrocatalytic current measurements to follow oxygen reduction coupled to proton uptake in cytochrome c oxidase isolated from Paracoccus denitrificans. Wild type enzyme and site-specific variants with defects in both proton uptake pathways (K354M, D124N and K354M/D124N) were immobilized on gold nanoparticles, and oxygen reduction was probed electrochemically in the presence of varying concentrations of Zn2+ ions, which are known to inhibit both the entry and the exit proton pathways in the enzyme. Our data suggest that under these conditions substrate protons gain access to the oxygen reduction site via the exit pathway.

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Language(s): eng - English
 Dates: 2015-01-052014-11-262015-01-072015-01-282015-02-27
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.febslet.2015.01.014
 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: 589 (5) Sequence Number: - Start / End Page: 565 - 568 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501