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  Identification and characterization of the novel subunit CcoM in the cbb3-cytochrome c oxidase from Pseudomonas stutzeri ZoBell

Kohlstädt, M., Buschmann, S., Xie, H., Resemann, A., Warkentin, E., Langer, J. D., et al. (2016). Identification and characterization of the novel subunit CcoM in the cbb3-cytochrome c oxidase from Pseudomonas stutzeri ZoBell. mBio, 7(7), 1-9. doi:10.1128/mBio.01921-15.

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 Creators:
Kohlstädt, Martin1, Author              
Buschmann, Sabine1, Author              
Xie, Hao1, Author              
Resemann, Anja2, Author
Warkentin, Eberhard1, Author              
Langer, Julian David1, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Bruker Daltonik GmbH, Bremen, Germany, ou_persistent22              

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 Abstract: Cytochrome c oxidases (CcOs), members of the heme-copper containing oxidase (HCO) superfamily, are the terminal enzymes of aerobic respiratory chains. The cbb3-type cytochrome c oxidases (cbb3-CcO) form the C-family and have only the central catalytic subunit in common with the A- and B-family HCOs. In Pseudomonas stutzeri, two cbb3 operons are organized in a tandem repeat. The atomic structure of the first cbb3 isoform (Cbb3-1) was determined at 3.2 Å resolution in 2010 (S. Buschmann, E. Warkentin, H. Xie, J. D. Langer, U. Ermler, and H. Michel, Science 329:327–330, 2010, http://dx.doi.org/10.1126/science.1187303). Unexpectedly, the electron density map of Cbb3-1 revealed the presence of an additional transmembrane helix (TMH) which could not be assigned to any known protein. We now identified this TMH as the previously uncharacterized protein PstZoBell_05036, using a customized matrix-assisted laser desorption ionization (MALDI)–tandem mass spectrometry setup. The amino acid sequence matches the electron density of the unassigned TMH. Consequently, the protein was renamed CcoM. In order to identify the function of this new subunit in the cbb3 complex, we generated and analyzed a CcoM knockout strain. The results of the biochemical and biophysical characterization indicate that CcoM may be involved in CcO complex assembly or stabilization. In addition, we found that CcoM plays a role in anaerobic respiration, as the ΔCcoM strain displayed altered growth rates under anaerobic denitrifying conditions

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Language(s): eng - English
 Dates: 2015-12-092015-12-212016-01-26
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1128/mBio.01921-15
 Degree: -

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Title: mBio
Source Genre: Journal
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Publ. Info: Washington, DC : American Society for Microbiology
Pages: - Volume / Issue: 7 (7) Sequence Number: - Start / End Page: 1 - 9 Identifier: Other: 2150-7511
CoNE: https://pure.mpg.de/cone/journals/resource/2150-7511