Abstract
Cell respiration is catalyzed by the heme-copper oxidase superfamily of enzymes, which comprises cytochrome c and ubiquinol oxidases. These membrane proteins utilize different electron donors through dissimilar access mechanisms. We report here the first structure of a ubiquinol oxidase, cytochrome bo3, from Escherichia coli. The overall structure of the enzyme is similar to those of cytochrome c oxidases; however, the membrane-spanning region of subunit I contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in the cytochrome c oxidase. Mutagenesis studies on these residues strongly suggest that this region forms a quinone binding site. A sequence comparison of this region with known quinone binding sites in other membrane proteins shows remarkable similarities. In light of these findings we suggest specific roles for these polar residues in electron and proton transfer in ubiquinol oxidase.
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Acknowledgements
This work was supported by the EU Biotechnology Program and grants from the Academy of Finland, University of Helsinki (to M.W.), and the Swedish Research Councils, NFR and MFR (to S.I.). We are grateful to J. Hajdu and M.I. Verkhovsky for helpful discussions, B. Byrne and M. Nervall for figure preparation; and to A. Garcia-Horsman for contributions at an early stage of this work. We would also like to thank Hoffman-LaRoche, Switzerland, for the kind gift of ubiquinone-1.
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Abramson, J., Riistama, S., Larsson, G. et al. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Mol Biol 7, 910–917 (2000). https://doi.org/10.1038/82824
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DOI: https://doi.org/10.1038/82824
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