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ID 20663
本文ファイル
著者
Kawamura, Izuru
Degawa, Yoshiaki
Yamaguchi, Satoru
Nishimura, Katsuyuki
Tuzi, Satoru
Saito, Hazime
Naito, Akira
NDC
生物科学・一般生物学
抄録(英)
Bacteriorhodopsin (bR), a retinal protein in purple membrane of H.salinarum, shows functions as a light-driven proton pump. We have detected pressure induced isomerization of retinal in bR by 15N cross polarization-magic angle spinning (CP-MAS) NMR spectra of [ε-15N]Lys-labeled bR. In the 15N NMR spectra, both all-trans and 13-cis retinal configurations have been observed at 148.0 and 155.0 ppm, respectively, at the MAS frequency of 4 kHz in the dark. When the MAS frequency was increased up to 12 kHz corresponding to the sample pressure of 80 atm, the 15N NMR signals of Schiff Base of retinal were broadened. The signal intensity of 13-cis retinal at 155.0 ppm was increased when the MAS frequency was decreased from 12 kHz to 4 kHz. These results showed that the equilibrium constant of [13-cis –bR] /[all-trans-bR] increased by the pressure of 80 atm. It was also revealed that the changes induced by the pressure were quite local. Therefore, microscopically, hydrogen-bond network around retinal would be disrupted or distorted by a constantly applied pressure. It is, therefore, clearly demonstrated that increased pressure induced by fast MAS frequencies generated 13-cis isomerization of retinal in the membrane protein bR.
掲載誌名
Photochemistry and Photobiology
83巻
2号
開始ページ
346
終了ページ
350
出版年月日
2007-03
出版者
American Society of Photobiology
ISSN
0031-8655
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
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権利情報
Author Posting. (c) The Authors (2007) This is the author's version of the work. It is posted here for personal use, not for redistribution. The definitive version was published in PHOTOCHEMISTRY AND PHOTOBIOLOGY, 83(2): 346-350. http://dx.doi.org/10.1562/2006-06-20-RC-941
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