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Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome c oxidase.
Safari, Cecilia; Ghosh, Swagatha; Andersson, Rebecka; Johannesson, Jonatan; Båth, Petra; Uwangue, Owens; Dahl, Peter; Zoric, Doris; Sandelin, Emil; Vallejos, Adams; Nango, Eriko; Tanaka, Rie; Bosman, Robert; Börjesson, Per; Dunevall, Elin; Hammarin, Greger; Ortolani, Giorgia; Panman, Matthijs; Tanaka, Tomoyuki; Yamashita, Ayumi; Arima, Toshi; Sugahara, Michihiro; Suzuki, Mamoru; Masuda, Tetsuya; Takeda, Hanae; Yamagiwa, Raika; Oda, Kazumasa; Fukuda, Masahiro; Tosha, Takehiko; Naitow, Hisashi; Owada, Shigeki; Tono, Kensuke; Nureki, Osamu; Iwata, So; Neutze, Richard; Brändén, Gisela.
Affiliation
  • Safari C; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Ghosh S; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Andersson R; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Johannesson J; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Båth P; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Uwangue O; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Dahl P; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Zoric D; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Sandelin E; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Vallejos A; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Nango E; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Tanaka R; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
  • Bosman R; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Börjesson P; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
  • Dunevall E; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Hammarin G; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Ortolani G; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Panman M; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Tanaka T; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Yamashita A; Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
  • Arima T; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Sugahara M; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Suzuki M; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Masuda T; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Takeda H; Laboratory of Supramolecular Crystallography, Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, Osaka, Japan.
  • Yamagiwa R; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.
  • Oda K; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Fukuda M; Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori, Ako, Hyogo 678-1297, Japan.
  • Tosha T; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Naitow H; Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori, Ako, Hyogo 678-1297, Japan.
  • Owada S; Department of Biological Sciences, Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
  • Tono K; Department of Biological Sciences, Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
  • Nureki O; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Iwata S; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Neutze R; RIKEN SPring-8 Center, 1-1-1 Kuoto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
  • Brändén G; Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Sci Adv ; 9(49): eadh4179, 2023 Dec 08.
Article in En | MEDLINE | ID: mdl-38064560
ABSTRACT
Cytochrome c oxidase (CcO) 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 a3 of ba3-type CcO. In contrast with the aa3-type enzyme, our data show how CO is stabilized on CuB through interactions with a transiently ordered water molecule. These results offer a structural explanation for the extended lifetime of the CuB-CO complex in ba3-type CcO and, by extension, the extremely high oxygen affinity of the enzyme.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carbon Monoxide / Electron Transport Complex IV Language: En Journal: Sci Adv Year: 2023 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carbon Monoxide / Electron Transport Complex IV Language: En Journal: Sci Adv Year: 2023 Document type: Article Affiliation country: