E
Eiki Yamashita
Researcher at Osaka University
Publications - 151
Citations - 13325
Eiki Yamashita is an academic researcher from Osaka University. The author has contributed to research in topics: Cytochrome c oxidase & Cytochrome b6f complex. The author has an hindex of 43, co-authored 145 publications receiving 12239 citations. Previous affiliations of Eiki Yamashita include Purdue University & Kwansei Gakuin University.
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Journal ArticleDOI
The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A.
Tomitake Tsukihara,Hiroshi Aoyama,Eiki Yamashita,Takashi Tomizaki,Hiroshi Yamaguchi,Kyoko Shinzawa-Itoh,Ryosuke Nakashima,Rieko Yaono,Shinya Yoshikawa +8 more
TL;DR: Two possible proton pathways for pumping, each spanning from the matrix to the cytosolic surfaces, were identified, including hydrogen bonds, internal cavities likely to contain water molecules, and structures that could form hydrogen bonds with small possible conformational change of amino acid side chains.
Journal ArticleDOI
Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A
Tomitake Tsukihara,Hiroshi Aoyama,Eiki Yamashita,Takashi Tomizaki,Hiroshi Yamaguchi,Kyoko Shinzawa-Itoh,Ryosuke Nakashima,Rieko Yaono,Shinya Yoshikawa +8 more
TL;DR: The high resolution three-dimensional x-ray structure of the metal sites of bovine heart cytochrome c oxidase is reported, suggesting a dinuclear copper center with an unexpected structure similar to a [2Fe-2S]-type iron-sulfur center.
Journal ArticleDOI
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
Shinya Yoshikawa,Kyoko Shinzawa-Itoh,Ryosuke Nakashima,Rieko Yaono,Eiki Yamashita,Noriko Inoue,Min Yao,Ming Jie Fei,Clare Peters Libeu,Tsunehiro Mizushima,Hiroshi Yamaguchi,Takashi Tomizaki,Tomitake Tsukihara +12 more
TL;DR: Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.35, 2.9, and 2.8 angstrom resolution, indicating the aspartate as the as partate pumping site for the O2 reduction by the enzyme.
Journal ArticleDOI
Crystal structure of bacterial multidrug efflux transporter AcrB
TL;DR: In this article, the crystal structure of AcrB at 3.5 A resolution was determined, which implies that substrates translocated from the cell interior through the transmembrane region and from the periplasm through the vestibules are collected in the central cavity and then actively transported through the pore into the TolC tunnel.
Journal ArticleDOI
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
TL;DR: AcrB as discussed by the authors is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA.