A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase | Zendy

Atsuhiro Shimada | Zendy; Minoru Kubo | Zendy; Seiki Baba | Zendy; Keitaro Yamashita | Zendy; Kunio Hirata | Zendy; Go Ueno | Zendy; Takashi Nomura | Zendy; Tetsunari Kimura | Zendy; Kyoko ShinzawaItoh | Zendy; Junpei Baba | Zendy; K. Hatano | Zendy; Y. Eto | Zendy; Akari Miyamoto | Zendy; Hironori Murakami | Zendy; Takashi Kumasaka | Zendy; Shigeki Owada | Zendy; Kensuke Tono | Zendy; Makina Yabashi | Zendy; Yoshihiro Yamaguchi | Zendy; Sachiko Yanagisawa | Zendy; Miyuki Sakaguchi | Zendy; Takashi Ogura | Zendy; Ryo Komiya | Zendy; Jiwang Yan | Zendy; Eiki Yamashita | Zendy; Masaki Yamamoto | Zendy; Hideo Ago | Zendy; Shinya Yoshikawa | Zendy; Tomitake Tsukihara | Zendy

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A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase

Author(s) -

Atsuhiro Shimada,

Minoru Kubo,

Seiki Baba,

Keitaro Yamashita,

Kunio Hirata,

Go Ueno,

Takashi Nomura,

Tetsunari Kimura,

Kyoko ShinzawaItoh,

Junpei Baba,

K. Hatano,

Y. Eto,

Akari Miyamoto,

Hironori Murakami,

Takashi Kumasaka,

Shigeki Owada,

Kensuke Tono,

Makina Yabashi,

Yoshihiro Yamaguchi,

Sachiko Yanagisawa,

Miyuki Sakaguchi,

Takashi Ogura,

Ryo Komiya,

Jiwang Yan,

Eiki Yamashita,

Masaki Yamamoto,

Hideo Ago,

Shinya Yoshikawa,

Tomitake Tsukihara

Publication year - 2017

Publication title -

science advances

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.928

H-Index - 146

ISSN - 2375-2548

DOI - 10.1126/sciadv.1603042

Subject(s) - nanosecond , backflow , heme , chemistry , heme a , cytochrome c oxidase , proton , photochemistry , bicarbonate , biophysics , laser , optics , biochemistry , enzyme , physics , biology , mechanical engineering , organic chemistry , quantum mechanics , inlet , engineering

Bovine cytochrome c oxidase (CcO), a 420-kDa membrane protein, pumps protons using electrostatic repulsion between protons transferred through a water channel and net positive charges created by oxidation of heme a (Fe-a) for reduction of O-2 at heme a(3) (Fe-a3). For this process to function properly, timing is essential: The channel must be closed after collection of the protons to be pumped and before Fea oxidation. If the channel were to remain open, spontaneous backflow of the collected protons would occur. For elucidation of the channel closure mechanism, the opening of the channel, which occurs upon release of CO from CcO, is investigated by newly developed time-resolved x-ray free-electron laser and infrared techniques with nanosecond time resolution. The opening process indicates that Cu-B senses completion of proton collection and binds O-2 before binding to Fe-a3 to close the water channel using a conformational relay system, which includes Cu-B, heme a(3), and a transmembrane helix, to block backflow of the collected protons

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