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Journal of Bacteriology, August 2008, p. 5576-5586, Vol. 190, No. 16
0021-9193/08/$08.00+0     doi:10.1128/JB.00534-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Stability of the cbb3-Type Cytochrome Oxidase Requires Specific CcoQ-CcoP Interactions{triangledown}

Annette Peters,1 Carmen Kulajta,1 Grzegorz Pawlik,1 Fevzi Daldal,2 and Hans-Georg Koch1*

Zentrum für Biochemie und Molekulare Zellforschung, Institut für Biochemie und Molekularbiologie, Albert-Ludwigs-Universität Freiburg, Stefan-Maier-Str. 17, 79104 Freiburg, Germany,1 Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 191042

Received 18 April 2008/ Accepted 4 June 2008

Cytochrome cbb3-type oxidases are members of the heme copper oxidase superfamily and are composed of four subunits. CcoN contains the heme b-CuB binuclear center where oxygen is reduced, while CcoP and CcoO are membrane-bound c-type cytochromes thought to channel electrons from the donor cytochrome into the binuclear center. Like many other bacterial members of this superfamily, the cytochrome cbb3-type oxidase contains a fourth, non-cofactor-containing subunit, which is termed CcoQ. In the present study, we analyzed the role of CcoQ on the stability and activity of Rhodobacter capsulatus cbb3-type oxidase. Our data showed that CcoQ is a single-spanning membrane protein with a Nout-Cin topology. In the absence of CcoQ, cbb3-type oxidase activity is significantly reduced, irrespective of the growth conditions. Blue native polyacrylamide gel electrophoresis analyses revealed that the lack of CcoQ specifically impaired the stable recruitment of CcoP into the cbb3-type oxidase complex. This suggested a specific CcoQ-CcoP interaction, which was confirmed by chemical cross-linking. Collectively, our data demonstrated that in R. capsulatus CcoQ was required for optimal cbb3-type oxidase activity because it stabilized the interaction of CcoP with the CcoNO core complex, leading subsequently to the formation of the active 230-kDa cbb3-type oxidase complex.

* Corresponding author. Mailing address: Zentrum für Biochemie und Molekulare Zellforschung, Institut für Biochemie und Molekularbiologie, Albert-Ludwigs-Universität Freiburg, Stefan-Maier-Str. 17, 79104 Freiburg, Germany. Phone: 0049 761 2035250. Fax: 0049 761 2035289. E-mail: Hans-Georg.Koch{at}biochemie.uni-freiburg.de

{triangledown} Published ahead of print on 13 June 2008.

Journal of Bacteriology, August 2008, p. 5576-5586, Vol. 190, No. 16
0021-9193/08/$08.00+0     doi:10.1128/JB.00534-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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