Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Rebecka Andersson, Cecilia Safari, Robert Dods, Eriko Nango, Rie Tanaka, Ayumi Yamashita, Takanori Nakane, Kensuke Tono, Yasumasa Joti, Petra Båth, Elin Dunevall, Robert Bosman, Osamu Nureki, So Iwata, Richard Neutze, Gisela Brändén

ABSTRACT

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 2.3 Å 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. More... »

PAGES

4518

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-017-04817-z

DOI

http://dx.doi.org/10.1038/s41598-017-04817-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1090334009

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28674417


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