|
JAIST Repository >
School of Materials Science >
Articles >
Journal Articles >
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)
|
Files in This Item:
File |
Description |
Size | Format |
C9743.pdf | | 725Kb | Adobe PDF | View/Open |
|
All items in DSpace are protected by copyright, with all rights reserved.
|