To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

Serial femtosecond crysta… - University of Gothenburg, Sweden Till startsida
Sitemap
To content Read more about how we use cookies on gu.se

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

Journal article
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
Published in Scientific reports
Volume 7
Issue 1
Pages 4518
ISSN 2045-2322
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 4518
Language en
Links dx.doi.org/10.1038/s41598-017-04817...
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Biochemistry, Structural Biology

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.

Page Manager: Webmaster|Last update: 9/11/2012
Share:

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?

Denna text är utskriven från följande webbsida:
http://www.gu.se/english/research/publication/?publicationId=255358
Utskriftsdatum: 2019-08-21