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

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.

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 Creators:
Iwata, So1, Author           
Ostermeier, Christian1, Author           
Ludwig, Bernd2, Author
Michel, Hartmut1, Author                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Johann-Wolfgang-Goethe Universität, Biozentrum, Institut für Biochemie, Molekulare Genetik, Frankfurt/M., Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 1995-07-191995-08-031995-08-24
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/376660a0
 Degree: -

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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 376 (6542) Sequence Number: - Start / End Page: 660 - 669 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238