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细菌视紫红质的质子传输机理
引用本文:王丽萍,李宝芳,江龙.细菌视紫红质的质子传输机理[J].生物化学与生物物理进展,2001,28(3):279-282.
作者姓名:王丽萍  李宝芳  江龙
作者单位:中国科学院化学研究所,分子科学中心,
摘    要:细菌视紫红质(bR)是嗜盐菌紫膜中的唯一蛋白质成分, 具有质子泵、电荷分离和光致变色功能. bR分子中的发色团视黄醛通过质子化席夫碱以共价键与Lys216相连. bR分子受可见光照射后, 视黄醛发生从全-反到13-顺式构型的异构化, 导致席夫碱的去质子化,继之以可极化基团位置的改变. 力场的变化引起包括蛋白质三级结构在内的诸多变化, 这些变化促进并保证了质子从细胞质侧向细胞外侧的定向传输.

关 键 词:细菌视紫红质,质子传输    视黄醛,异构化,M态
收稿时间:1/5/2001 12:00:00 AM
修稿时间:2001年1月5日

Molecular Mechanism for Proton Translocation of Bacteriorhodopsin
WANG Li-Ping,LI Bao-Fang and JIANG Long.Molecular Mechanism for Proton Translocation of Bacteriorhodopsin[J].Progress In Biochemistry and Biophysics,2001,28(3):279-282.
Authors:WANG Li-Ping  LI Bao-Fang and JIANG Long
Institution:Center for Molecular Science, Institute of Chemistry, The Chinese Academy of Sciences, Beijing 100080, China;Center for Molecular Science, Institute of Chemistry, The Chinese Academy of Sciences, Beijing 100080, China;Center for Molecular Science, Institute of Chemistry, The Chinese Academy of Sciences, Beijing 100080, China
Abstract:Bacteriorhodopsin (bR) is the sole protein in the purple membrane of Halobacterium salinarium, which functions as proton pump, charge separation and photochromism. The chromophore retinal is covalently attached to Lys 216 via a protonated Schiff base. Upon illumination, the all-trans to 13-cis isomerization of the retinal results in deprotonation of the Schiff base followed by alterations in protonatable groups within bacteriorhodopsin. The changed force field induces changes, even in the tertiary structure, which facilitate and warrant the vectorial proton translocation.
Keywords:bacteriorhodopsin  proton translocation  retinal  isomerization  M intermediate
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