-
- 神山 勉
- 名古屋大学大学院理学研究科
書誌事項
- タイトル別名
-
- Four-Dimensional X-ray Crystallography of Light-Driven Proton Pumps
- サイキン ノ ケンキュウ カラ ヒカリ クドウ プロトン ポンプ ノ 4ジゲン Xセン コウゾウ カイセキ
この論文をさがす
抄録
Bacteriorhodopsin (bR), a membrane protein found in Halobacterium salinarum, contains retinal as chromophore and functions as a light-driven proton pump. We have carried out four-dimensional X-ray crystallographic studies of bR and its homologous proteins, to elucidate the proton pumping mechanism. A novel crystallization method, called the membrane fusion method, has been developed to prepare a 3D crystal that is stable over a wide pH range. This enabled us to investigate pH-induced as well as light-induced structural changes. Structural analyses of reaction intermediates revealed that water relocation, which affects the pKa values of ionizable residues in the proton channel, takes place in the early stage of the proton pumping cycle. On the basis of this observation, we hypothesized that bR is a water/proton anti-porter. Since some of internal cavities are highly conserved during the evolution, it is suggested that their morphological changes initiated by the retinal photo-isomerization play an important role for water relocation and proton tranlocation across the membrane.
収録刊行物
-
- 日本結晶学会誌
-
日本結晶学会誌 48 (5), 359-366, 2006
日本結晶学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390001204087325568
-
- NII論文ID
- 10018331312
-
- NII書誌ID
- AN00188364
-
- ISSN
- 18845576
- 03694585
-
- NDL書誌ID
- 8564086
-
- 本文言語コード
- ja
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可