2000年10月
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site
NATURE STRUCTURAL BIOLOGY
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- 巻
- 7
- 号
- 10
- 開始ページ
- 910
- 終了ページ
- 917
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/82824
- 出版者・発行元
- NATURE AMERICA INC
Cell respiration is catalyzed by the heme-copper oxidase superfamily of enzymes, which comprises cytochrome c and ubiquinol oxidases, These membrane proteins utilize different electron donors through dissimilar access mechanisms. We report here the first structure of a ubiquinol oxidase, cytochrome bo(3), from Escherichia coli, The overall structure of the enzyme is similar to those of cytochrome c oxidases; however, the membrane-spanning region of subunit I contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in the cytochrome c oxidase, Mutagenesis studies on these residues strongly suggest that this region forms a quinone binding site. A sequence comparison of this region with known quinone binding sites in other membrane proteins shows remarkable similarities. In light of these findings we suggest specific roles for these polar residues in electron and proton transfer in ubiquinol oxidase.
- リンク情報
- ID情報
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- DOI : 10.1038/82824
- ISSN : 1072-8368
- Web of Science ID : WOS:000089779900023