The dependence of pH and ionic strength of kinetic absorption spectroscopy of acetylated bacteriorhodopsin  

The dependence of pH and ionic strength of kinetic absorption spectroscopy of acetylated bacteriorhodopsin

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作  者:王光毓 胡坤生 

机构地区:[1]Comprehensive Technology Institure,Capiral Norrul University, Beijing 100101. China [2]Institute of Biophysics. Chinese Academy of Sciences, Beijing 100101. China

出  处:《Chinese Science Bulletin》1995年第18期1558-1561,共4页

基  金:Project supported by the Key Foundation of Chinese Academy of Sciences.

摘  要:Bacteriorhodopsin (bR) in purple membrane (PM) from H. Halobium is a light-drivenproton pump. Its seven transmembrane helices form an internal proton channel. Anall-trans retinal covalently links up via protonated Schiff base with K216 inside thechannel. Upon illumination, the retinal isomerization around the C<sub>13</sub>-C<sub>14</sub> double bond drivesprotons translocation through the channel from the cytoplasm into the medium, and

关 键 词:BACTERIORHODOPSIN ACETYLATION surface CHARGE INTERMEDIATE M412. 

分 类 号:Q63[生物学—生物物理学]

 

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