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  • Andersson, Rebecka,1988Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology (author)

Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.

  • Article/chapterEnglish2017

Publisher, publication year, extent ...

  • 2017-07-03
  • Springer Science and Business Media LLC,2017

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/255358
  • https://gup.ub.gu.se/publication/255358URI
  • https://doi.org/10.1038/s41598-017-04817-zDOI

Supplementary language notes

  • Language:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Cytochrome c oxidase catalyses the reduction of molecular oxygen to water while the energy released in this process is used to pump protons across a biological membrane. Although an extremely well-studied biological system, the molecular mechanism of proton pumping by cytochrome c oxidase is still not understood. Here we report a method to produce large quantities of highly diffracting microcrystals of ba 3-type cytochrome c oxidase from Thermus thermophilus suitable for serial femtosecond crystallography. The room-temperature structure of cytochrome c oxidase is solved to 2.3Å resolution from data collected at an X-ray Free Electron Laser. We find overall agreement with earlier X-ray structures solved from diffraction data collected at cryogenic temperature. Previous structures solved from synchrotron radiation data, however, have shown conflicting results regarding the identity of the active-site ligand. Our room-temperature structure, which is free from the effects of radiation damage, reveals that a single-oxygen species in the form of a water molecule or hydroxide ion is bound in the active site. Structural differences between the ba 3-type and aa 3-type cytochrome c oxidases around the proton-loading site are also described.

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  • Safari, Cecilia,1989Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xsafce (author)
  • Dods, Robert,1989Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xdodsr (author)
  • Nango, Eriko (author)
  • Tanaka, Rie (author)
  • Yamashita, Ayumi (author)
  • Nakane, Takanori (author)
  • Tono, Kensuke (author)
  • Joti, Yasumasa (author)
  • Båth, Petra,1988Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbatpe (author)
  • Dunevall, Elin,1986Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xjelix (author)
  • Bosman, Robert,1991Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbosro (author)
  • Nureki, Osamu (author)
  • Iwata, So (author)
  • Neutze, Richard,1969Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xneuri (author)
  • Brändén, Gisela,1975Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbragi (author)
  • Göteborgs universitetInstitutionen för kemi och molekylärbiologi (creator_code:org_t)

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  • In:Scientific reports: Springer Science and Business Media LLC7:12045-2322

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