Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature

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 i...

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/cd8cd5af252c472fa3951c2976f0f994
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spelling	oai:doaj.org-article:cd8cd5af252c472fa3951c2976f0f9942021-12-02T11:41:01ZSerial femtosecond crystallography structure of cytochrome c oxidase at room temperature10.1038/s41598-017-04817-z2045-2322https://doaj.org/article/cd8cd5af252c472fa3951c2976f0f9942017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04817-zhttps://doaj.org/toc/2045-2322Abstract 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.Rebecka AnderssonCecilia SafariRobert DodsEriko NangoRie TanakaAyumi YamashitaTakanori NakaneKensuke TonoYasumasa JotiPetra BåthElin DunevallRobert BosmanOsamu NurekiSo IwataRichard NeutzeGisela BrändénNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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 Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
description	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.
format	article
author	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
author_facet	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
author_sort	Rebecka Andersson
title	Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
title_short	Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
title_full	Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
title_fullStr	Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
title_full_unstemmed	Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
title_sort	serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/cd8cd5af252c472fa3951c2976f0f994
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_version_	1718395485682663424

Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature

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