Culture Temperature Affects the Molecular Motion of Bacteriorhodopsin within the Purple Membrane
スポンサーリンク
概要
- 論文の詳細を見る
We measured the absorption anisotropies of bacteriorhodopsin (bR) within a purple membrane suspension after photo-excitation in the millisecond time range. The purple membranes used were isolated from Halobacterium salinarium grown at three different culture temperatures, 37.0,43.0 and 47.5℃. For the membranes from the 37.0℃ culture, the observed anisotropies at wavelengths of 410,570 and 680 nm showed almost the same slow decay. The slow decaying of the anisotropies originated from the rotation of the membrane itself. Using the membranes from the 43.0 and 47.5℃ culture, however, we found that the anisotropy change varied at each wavelength measured. In these cases, it is shown from detailed data analysis that 1) the rotational motion of photo-intermediates within the membrane is more restricted than that of non-excited bR and 2) the distorted arrangements of the proteins within the membrane remain, even after photo-intermediates return to ground-state bR. This restricted motion is probably caused by the conformational changes in photo-intermediates, which prevent the rotation of the monomer protein and/or lead photo-intermediates to bind with neighboring proteins.
- 社団法人日本薬学会の論文
- 1996-03-15
著者
-
Kamo Naoki
Faculty of Advanced Life Science, Hokkaido University
-
Kouno T
Faculty Of Pharmaceutical Sciences University Of Toyama
-
KIKUKAWA Takashi
Research Institute for Electronic Science, Hollaido University
-
ARAISO Tsunehisa
Research Institute for Electronic Science, Hollaido University
-
MUKASA Koichi
Faculty of Engineering, Hollaido University
-
SHIMOZAWA Tateo
Research Institute for Electronic Science, Hollaido University
-
水谷 忠士
Faculty Of Advanced Life Science Hokkaido University
-
Mukasa Koichi
Faculty Of Engineering Hollaido University
-
Kamo Naoki
Faculty Of Advanced Life Science Hokkaido University
-
Kamo Naoki
Laboratory Of Biophysical Chemistry Faculty Of Advanced Life Science Hokkaido University
-
Shimozawa Tateo
Research Institute For Electronic Science Hollaido University
-
Kamo Naoki
Faculty Of Pharmaceutical Sciences Grad. School Of Pharmaceutical Siences Hokkaido Univ.
-
Kamo Naoki
Facultu Of Pharmaceutics Hokkaido University
-
Kamo Naoki
College Of Pharmaceutical Science Matsuyama University Matsuyama Japan
関連論文
- Heterologous Expression of Pharaonis Halorhodopsin in Xenopus laevis Oocytes and Electrophysiological Characterization of Its Light-Driven Cl- Pump Activity
- Interaction of the Halobacterial Transducer to a Halorhodopsin Mutant Engineered so as to Bind the Transducer : Cl- Circulation within the Extracellular Channel
- Participation of the surface structure of pharaonis phoborhodopsin, ppR and its A149S and A149V mutants, consisting of the C-terminal α-helix and E-F loop, in the complex-formation with the cognate transducer pHtrII, as revealed by site-directed 13C solid
- Importance of specific hydrogen bonds of archaeal rhodopsins for the binding to the transducer protein†
- 2P313 Structural network in the extracellular region corresponding to the visual spectral shift of halorhodopsin(41. Proton and ion pumping,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 2P311 The role of E234 on the extracellular site in the anion pump of pharaonis halorhodopsin(41. Proton and ion pumping,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- Role of Arg-72 of pharaonis Phoborhodopsin (sensory rhodopsin II) on its photochemistry.
- Role of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II).
- Association between a photo-intermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer.
- 1P423 Local Conformation and Dynamics Changes in the vicinity of the Retinal in Photoactivated pharaonis phoborhodopsin by Solid-State NMR(17. Light driven system,Poster Session,Abstract,Meeting Program of EABS &BSJ 2006)