Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome <i>c</i> oxidase-Reference-Cited by-同舟云学术

Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome c oxidase

Published:2023-12-08 Issue:49 Volume:9 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Safari Cecilia¹^ORCID,Ghosh Swagatha¹^ORCID,Andersson Rebecka¹^ORCID,Johannesson Jonatan¹^ORCID,Båth Petra¹^ORCID,Uwangue Owens¹,Dahl Peter¹,Zoric Doris¹^ORCID,Sandelin Emil¹^ORCID,Vallejos Adams¹^ORCID,Nango Eriko²³^ORCID,Tanaka Rie²³^ORCID,Bosman Robert¹^ORCID,Börjesson Per¹,Dunevall Elin¹,Hammarin Greger¹^ORCID,Ortolani Giorgia¹^ORCID,Panman Matthijs¹^ORCID,Tanaka Tomoyuki²,Yamashita Ayumi²^ORCID,Arima Toshi²,Sugahara Michihiro²,Suzuki Mamoru⁴,Masuda Tetsuya⁵^ORCID,Takeda Hanae²⁶,Yamagiwa Raika²⁶,Oda Kazumasa⁷^ORCID,Fukuda Masahiro⁷^ORCID,Tosha Takehiko²^ORCID,Naitow Hisashi²,Owada Shigeki²⁸^ORCID,Tono Kensuke²⁸^ORCID,Nureki Osamu⁷^ORCID,Iwata So²³^ORCID,Neutze Richard¹^ORCID,Brändén Gisela¹^ORCID

Affiliation:

1. Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.

2. RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

3. Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.

4. Laboratory of Supramolecular Crystallography, Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, Osaka, Japan.

5. Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.

6. Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori, Ako, Hyogo 678-1297, Japan.

7. Department of Biological Sciences, Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.

8. Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.

Abstract

Cytochrome c oxidase (C c O) is part of the respiratory chain and contributes to the electrochemical membrane gradient in mitochondria as well as in many bacteria, as it uses the energy released in the reduction of oxygen to pump protons across an energy-transducing biological membrane. Here, we use time-resolved serial femtosecond crystallography to study the structural response of the active site upon flash photolysis of carbon monoxide (CO) from the reduced heme a 3 of ba 3 -type C c O. In contrast with the aa 3 -type enzyme, our data show how CO is stabilized on Cu B through interactions with a transiently ordered water molecule. These results offer a structural explanation for the extended lifetime of the Cu B -CO complex in ba 3 -type C c O and, by extension, the extremely high oxygen affinity of the enzyme.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Link

https://www.science.org/doi/pdf/10.1126/sciadv.adh4179

Reference81 articles.

1. Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism

2. Proton pump coupled to cytochrome c oxidase in mitochondria

3. Proton-Coupled Electron Transfer in Cytochrome Oxidase

4. Glutamate 286 in Cytochrome aa3 from Rhodobacter sphaeroides Is Involved in Proton Uptake during the Reaction of the Fully-Reduced Enzyme with Dioxygen

5. On the role of the K-proton transfer pathway in cytochrome c oxidase

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