ACTIVE-SITE STRUCTURE OF BACTERIORHODOPSIN AND MECHANISM OF ACTION

被引:9
作者
CRESPI, HL
FERRARO, JR
机构
[1] Chemistry Division, Argonne National Laboratory Argonne
关键词
D O I
10.1016/0006-291X(79)91561-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Pressure experiments with freeze-dried bacteriorhodopsin indicate that water is an essential part of the chromophore. This observation is combined with already known information on (a) the pH dependence of proton pumping, (b) the secondary protein-chromophore interaction with lysine-40, and (c) the proton transfer in the initial photochemical step to give a detailed structure of the active site and a mechanism for proton pumping which is consistent with the bacteriorhodopsin polypeptide sequence. © 1979.
引用
收藏
页码:575 / 582
页数:8
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