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Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans

Nature volume ?376 ,? pages 660?669 ( 1995 ) Cite this article

Abstract

The crystal structure at 2.8 A resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans , complexed with an antibody F v fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a 3 -copper B binuclear centre where molecular oxygen is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be identified. Mechanisms for proton pumping are discussed.

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Authors and Affiliations

  1. Max-Planck-lnstitut fur Biophysik, Heinrich-Hoffmann-Strasse 7, D-60528, Frankfurt/M., Germany

    So Iwata,?Christian Ostermeier?&?Hartmut Michel

  2. Johann-Wolfgang-Goethe Universitat, Biozentrum, Institut fur Biochemie, Molekulare Genetik, Marie-Curie-Strasse 9, D-60439, Frankfurt/M., Germany

    Bernd Ludwig

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  1. So Iwata
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  2. Christian Ostermeier
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  3. Bernd Ludwig
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  4. Hartmut Michel
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Iwata, S., Ostermeier, C., Ludwig, B. et al. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans . Nature 376 , 660?669 (1995). https://doi.org/10.1038/376660a0

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