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Please use this identifier to cite or link to this item: http://hdl.handle.net/10119/4875

Title: Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase
Authors: Shinzawa-Itoh, Kyoko
Aoyama, Hiroshi
Muramoto, Kazumasa
Terada, Hirohito
Kurauchi, Tsuyoshi
Tadehara, Yoshiki
Yamasaki, Akiko
Sugimura, Takashi
Kurono, Sadamu
Tsujimoto, Kazuo
Mizushima, Tsunehiro
Yamashita, Eiki
Tsukihara, Tomitake
Yoshikawa, Shinya
Keywords: cytochrome c oxidase
fatty acid structure
mass spectrometry
phospholipids
X-ray structural analysis
Issue Date: 2007-03-21
Publisher: Nature Publishing Group
Magazine name: the EMBO Journal
Volume: 26
Number: 6
Start page: 1713
End page: 1725
DOI: 10.1038/sj.emboj.7601618
Abstract: All 13 lipids, including two cardiolipins, one phosphatidylcholine, three phosphatidylethanolamines, four phosphatidylglycerols and three triglycerides, were identified in a crystalline bovine heart cytochrome c oxidase (CcO) preparation. The chain lengths and unsaturated bond positions of the fatty acid moieties determined by mass spectrometry suggest that each lipid head group identifies its specific binding site within CcOs. The X-ray structure demonstrates that the flexibility of the fatty acid tails facilitates their effective space-filling functions and that the four phospholipids stabilize the CcO dimer. Binding of dicyclohexylcarbodiimide to the O_2 transfer pathway of CcO causes two palmitate tails of phosphatidylglycerols to block the pathway, suggesting that the palmitates control the O_2 transfer process. The phosphatidylglycerol with vaccenate (cis-Δ^<11>-octadecenoate) was found in CcOs of bovine and Paracoccus denitrificans, the ancestor of mitochondrion, indicating that the vaccenate is conserved in bovine CcO in spite of the abundance of oleate (cis-Δ^9-octadecenoate). The X-ray structure indicates that the protein moiety selects cis-vaccenate near the O_2 transfer pathway against trans-vaccenate. These results suggest that vaccenate plays a critical role in the O_2 transfer mechanism.
Rights: This is the author's version of the work. Copyright (C) 2007 European Molecular Biology Organization. K. Shinzawa-Itoh, H. Aoyama, K. Muramoto, H. Terada, T. Kurauchi, Y. Tadehara, A. Yamasaki, T. Sugimura, S. Kurono, K. Tsujimoto, T. Mizushima, E. Yamashita, T. Tsukihara and S. Yoshikawa, the EMBO Journal, 26(6), 2007, 1713-1725. http://dx.doi.org/10.1038/sj.emboj.7601618
URI: http://hdl.handle.net/10119/4875
Material Type: author
Appears in Collections:c10-1. 雑誌掲載論文 (Journal Articles)

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