A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase-Reference-Cited by-同舟云学术

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

Published:2017-07-07 Issue:7 Volume:3 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Shimada Atsuhiro¹,Kubo Minoru²³^ORCID,Baba Seiki⁴,Yamashita Keitaro²,Hirata Kunio²³,Ueno Go²,Nomura Takashi²^ORCID,Kimura Tetsunari⁵^ORCID,Shinzawa-Itoh Kyoko¹,Baba Junpei¹,Hatano Keita¹,Eto Yuki¹,Miyamoto Akari¹,Murakami Hironori⁴,Kumasaka Takashi⁴,Owada Shigeki²^ORCID,Tono Kensuke⁴^ORCID,Yabashi Makina⁴^ORCID,Yamaguchi Yoshihiro⁶,Yanagisawa Sachiko⁶,Sakaguchi Miyuki⁶,Ogura Takashi⁶,Komiya Ryo⁷,Yan Jiwang⁷,Yamashita Eiki⁸,Yamamoto Masaki²,Ago Hideo²,Yoshikawa Shinya¹^ORCID,Tsukihara Tomitake¹⁸⁹

Affiliation:

1. Picobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.

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

3. Japan Science and Technology Agency, Precursory Research for Embryonic Science and Technology (PRESTO), 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.

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

5. Graduate School of Science, Kobe University, 1-1 Rokkodai, Nada, Kobe, Hyogo 657-8501, Japan.

6. Picobiology Institute, Graduate School of Life Science, University of Hyogo, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.

7. Department of Mechanical Engineering, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.

8. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

9. Japan Science and Technology Agency, Core Research for Evolutional Science and Technology (CREST), 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.

Abstract

XFEL and IR analyses suggest that O 2 bound at Cu B blocks proton backflow for unidirectional H + transport by water channel closure.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference45 articles.

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3. Functions of the hydrophilic channels in protonmotive cytochrome c oxidase;Rich P. R.;J. R. Soc. Interface,2013

4. Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate;Muramoto K.;Proc. Natl. Acad. Sci. U.S.A.,2010

5. The Mg2+-containing water cluster of mammalian cytochrome c oxidase collects four pumping proton equivalents in each catalytic cycle;Yano N.;J. Biol. Chem.,2016

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