INVESTIGATION OF THE DYNAMICS OF BACTERIORHODOPSIN

被引:7
作者
PARAK, F
FISCHER, M
HEIDEMEIER, J
ENGELHARD, M
KOHL, KD
HESS, B
FORMANEK, H
机构
[1] MAX PLANCK INST ERNAHRUNGSPHYSIOL,W-4600 DORTMUND 1,GERMANY
[2] UNIV MUNICH,INST BOT,W-8000 MUNICH 2,GERMANY
来源
HYPERFINE INTERACTIONS | 1990年 / 58卷 / 1-4期
关键词
D O I
10.1007/BF02398348
中图分类号
O64 [物理化学(理论化学)、化学物理学]; O56 [分子物理学、原子物理学];
学科分类号
070203 ; 070304 ; 081704 ; 1406 ;
摘要
Bacteriorhodopsin (bR) converted to the blue form by deionization has been reconstituted to the active purple membrane by addition of57Fe ions. Mössbauer spectra measured in a wide temperature range reveal Fe3+ binding places with oxygen atoms in the neighbourhood. No evidence for a well defined functional binding place of the iron has been found. On a timescale faster 100 ns the purple membrane shows increasing flexibility above 200 K. In order to analyse the influence of the lipids, a bacteriorhodopsin sample where the lipid content has been increased artificially by the incorporation of DMPC as well as a sample consisting of lipid bilayer have been investigated. © 1990 J.C. Baltzer A.G. Scientific Publishing Company.
引用
收藏
页码:2381 / 2385
页数:5
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