Journal Article Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature

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

72017-07-03 , Springer Nature
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 ba3-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 ba3-type and aa3-type cytochrome c oxidases around the proton-loading site are also described.

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