5X1B

CO bound cytochrome c oxidase at 20 nsec after pump laser irradiation to release CO from O2 reduction center

Summary for 5X1B

• Entry DOI: 10.2210/pdb5x1b/pdb
• Related: 5X19 5X1F
• Descriptor: Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 7A1, mitochondrial, Cytochrome c oxidase subunit 7B, mitochondrial, ... (30 entities in total)
• Functional Keywords: cytochrome c oxidase, x-ray free electron laser, time-resolved analysis, proton pump, membrane protein, oxidoreductase
• Biological source: Bos taurus (Bovine); More
• Cellular location: Mitochondrion inner membrane; Multi-pass membrane protein: P00396 P68530 P00415; Mitochondrion inner membrane: P07470 P13183 P00430 P10175 P00423 P00426 P00428 P07471 P04038; Mitochondrion intermembrane space: P00429
• Total number of polymer chains: 26
• Total formula weight: 442964.12

Authors

Shimada, A.,Kubo, M.,Baba, S.,Yamashita, K.,Hirata, K.,Ueno, G.,Nomura, T.,Kimura, T.,Shinzawa-Itoh, K.,Baba, J.,Hatano, K.,Eto, Y.,Miyamoto, A.,Murakami, H.,Kumasaka, T.,Owada, S.,Tono, K.,Yabashi, M.,Yamaguchi, Y.,Yanagisawa, S.,Sakaguchi, M.,Ogura, T.,Komiya, R.,Yan, J.,Yamashita, E.,Yamamoto, M.,Ago, H.,Yoshikawa, S.,Tsukihara, T. (deposition date: 2017-01-25, release date: 2017-08-09, Last modification date: 2025-04-09)

Primary citation

Shimada, A.,Kubo, M.,Baba, S.,Yamashita, K.,Hirata, K.,Ueno, G.,Nomura, T.,Kimura, T.,Shinzawa-Itoh, K.,Baba, J.,Hatano, K.,Eto, Y.,Miyamoto, A.,Murakami, H.,Kumasaka, T.,Owada, S.,Tono, K.,Yabashi, M.,Yamaguchi, Y.,Yanagisawa, S.,Sakaguchi, M.,Ogura, T.,Komiya, R.,Yan, J.,Yamashita, E.,Yamamoto, M.,Ago, H.,Yoshikawa, S.,Tsukihara, T.
A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase.
Sci Adv, 3:e1603042-e1603042, 2017

PubMed Abstract: 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 (Fe ) for reduction of O at heme (Fe ). For this process to function properly, timing is essential: The channel must be closed after collection of the protons to be pumped and before Fe 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 senses completion of proton collection and binds O before binding to Fe to close the water channel using a conformational relay system, which includes Cu, heme , and a transmembrane helix, to block backflow of the collected protons.

PubMed: 28740863
DOI: 10.1126/sciadv.1603042

Experimental method

X-RAY DIFFRACTION (2.4 Å)