Chromophore/protein interaction in bacterial sensory rhodopsin and bacteriorhodopsin.
Chromophore/protein interaction in bacterial sensory rhodopsin and bacteriorhodopsin.
复制标题
细菌感觉视紫红质和细菌视紫红质中发色团/蛋白质的相互作用。
DOI：
10.1016/s0006-3495(86)83657-8
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发表时间：
1986
影响因子：
3.4
通讯作者：
Bogomolni,RA
中科院分区：
文献类型：
--
作者：
Spudich,JL;McCain,DA;Nakanishi,K;Okabe,M;Shimizu,N;Rodman,H;Honig,B;Bogomolni,RA
将具有改变共轭双键系统或改变立体化学的视网膜类似物掺入嗜盐嗜盐杆菌的趋光性受体感光视紫红质(SR)和光驱动质子泵细菌视紫红质(BR)中。由于与蛋白质微环境的模拟相互作用，吸收中的波长移动(“视蛋白移动”)表明，尽管两种蛋白质的功能不同，但它们的视网膜结合部位结构的整体静电和立体性质是相同的。根据视蛋白位移的PI电子计算得出了一种适用于SR和BR结合位置的蛋白质电荷分布的新描述。新的数据扩展了之前提出的BR的外部点电荷模型，包括了靠近β-紫罗兰酮部分的离子对蛋白质/发色团相互作用。新的数据修正了先前提出的外部点电荷模型，该模型的推导涉及一个BR类似物的实验错误的光学位移。
Retinal analogues with altered conjugated double bond systems or altered stereochemistry were incorporated into the phototaxis receptor sensory rhodopsin (SR) and the light-driven proton pump bacteriorhodopsin (BR) from Halobacterium halobium. Wavelength shifts in absorption ("opsin shifts") due to analogue interaction with the protein microenvironment demonstrate that the same overall electrostatic and steric properties of the retinal binding-site structures exist in both proteins despite their different functions. pi-Electron calculations from the opsin shifts lead to a new description of protein charge distribution that applies to the binding sites of both SR and BR. The new data extends the previously proposed external point charge model for BR to include an ion-pair protein/chromophore interaction near the beta-ionone moiety. The new data modifies the previously proposed external point-charge model, the derivation of which involved an experimentally erroneous opsin shift for one of the BR analogues.