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  Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase

Richter, O.-M.-H., Dürr, K. L., Kannt, A., Ludwig, B., Scandurra, F. M., Giuffrè, A., et al. (2005). Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase. The FEBS Journal, 272(2), 404-412. doi:10.1111/j.1742-4658.2004.04480.x.

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 Creators:
Richter, Oliver-M. H.1, Author
Dürr, Katharina L.2, Author           
Kannt, Aimo3, Author           
Ludwig, Bernd1, Author
Scandurra, Francesca M.4, Author
Giuffrè, Alessandro4, Author
Sarti, Paolo4, Author
Hellwig, Petra5, Author
Affiliations:
1Institut für Biochemie, Abteilung Molekulare Genetik, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany, ou_persistent22              
2Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
4Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome ‘La Sapienza’, Rome, Italy, ou_persistent22              
5Institut für Biophysik, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: cytochrome c oxidase; FTIR; proton channel; electron transfer; site‐directed mutagenesis
 Abstract: In recent studies on heme-copper oxidases a particular glutamate residue in subunit II has been suggested to constitute the entry point of the so-called K pathway. In contrast, mutations of this residue (E78II) in the Paracoccus denitrificans cytochrome c oxidase do not affect its catalytic activity at all (E78IIQ) or reduce it to about 50% (E78IIA); in the latter case, the mutation causes no drastic decrease in heme a3) reduction kinetics under anaerobic conditions, when compared to typical K pathway mutants. Moreover, both mutant enzymes retain full proton-pumping competence. While oxidized-minus-reduced Fourier-transform infrared difference spectroscopy demonstrates that E78II is indeed addressed by the redox state of the enzyme, absence of variations in the spectral range characteristic for protonated aspartic and glutamic acids at approximately 1760 to 1710 cm-1 excludes the protonation of E78II in the course of the redox reaction in the studied pH range, although shifts of vibrational modes at 1570 and 1400 cm-1 reflect the reorganization of its deprotonated side chain at pH values greater than 4.8. We therefore conclude that protons do not enter the K channel via E78II in the Paracoccus enzyme.

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Language(s): eng - English
 Dates: 2004-11-012004-08-232004-11-122004-12-212005-01-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1111/j.1742-4658.2004.04480.x
PMID: 15654878
 Degree: -

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Title: The FEBS Journal
  Other : The Federation if European Biochemical Societies Journal
Source Genre: Journal
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Publ. Info: Wiley-Blackwell
Pages: - Volume / Issue: 272 (2) Sequence Number: - Start / End Page: 404 - 412 Identifier: ISSN: 1742-464X
CoNE: https://pure.mpg.de/cone/journals/resource/954925398485