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Active site rearrangement and structural divergence in prokaryotic respiratory oxidases

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Safarian,  Schara
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hahn,  Alexander
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mills,  Deryck
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Radloff,  Melanie
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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

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Meier-Credo,  Jakob
Department of Structural 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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Kühlbrandt,  Werner
Department of Structural 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

Safarian, S., Hahn, A., Mills, D., Radloff, M., Eisinger, M. L., Nikolaev, A., et al. (2019). Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Science, 366(6461), 100-104. doi:10.1126/science.aay0967.


Cite as: http://hdl.handle.net/21.11116/0000-0004-C912-5
Abstract
Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo–electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily–specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.