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Subunit CcoQ is involved in the assembly of the Cbb3-type cytochrome c oxidases from Pseudomonas stutzeri ZoBell but not required for their activity

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Kohlstädt,  Martin
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Buschmann,  Sabine
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Xie,  Hao       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Kohlstädt, M., Buschmann, S., Langer, J. D., Xie, H., & Michel, H. (2017). Subunit CcoQ is involved in the assembly of the Cbb3-type cytochrome c oxidases from Pseudomonas stutzeri ZoBell but not required for their activity. Biochimica et Biophysica Acta, Bioenergetics, 1858(3), 231-238. doi:10.1016/j.bbabio.2016.12.006.


Cite as: https://hdl.handle.net/21.11116/0000-0000-6072-3
Abstract
The Cbb3-type cytochrome c oxidases (Cbb3-CcOs), the second most abundant CcOs, catalyze the reduction of molecular oxygen to water, even at micromolar oxygen concentrations. In Pseudomonas stutzeri ZoBell, two tandemly organized cbb3-operons encode the isoforms Cbb3-1 and Cbb3-2 both possessing subunits CcoN, CcoO and CcoP. However, only the cbb3-2 operon contains an additional ccoQ gene. CcoQ consists of 62 amino acids and is predicted to possess one transmembrane spanning helix. The physiological role of CcoQ was investigated based on a CcoQ-deletion mutant and wild-type Cbb3-2 crystals not containing subunit CcoQ. Cbb3-2 isolated from the deletion mutant is inactive and appears as a dispersed band on blue native-PAGE gels. Surprisingly, in the absence of ccoQ, Cbb3-1 also shows a strongly reduced activity. Our data suggest that CcoQ primarily functions as an assembly factor for Cbb3-2 but is also required for correct assembly of Cbb3-1. In contrast, once correctly assembled, Cbb3-1 and Cbb3-2 possess a full enzymatic activity even in the absence of CcoQ.