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

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Iwata,  So
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ostermeier,  Christian
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

Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature, 376(6542), 660-669. doi:10.1038/376660a0.


Cite as: http://hdl.handle.net/21.11116/0000-0006-C6CA-7
Abstract
The crystal structure at 2.8 Å resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a3-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.