Photolysis intermediates of the artificial visual pigment cis-5,6-dihydro-isorhodopsin.
Photolysis intermediates of the artificial visual pigment cis-5,6-dihydro-isorhodopsin.
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DOI：
10.1016/s0006-3495(89)82798-5
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发表时间：
1989-02
影响因子：
3.4
通讯作者：
Amnon Albeck;N. Friedman;M. Ottolenghi;M. Sheves;C. M. Einterz;S. Hug;J. W. Lewis;D. Kliger
中科院分区：
文献类型：
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作者：
Amnon Albeck;N. Friedman;M. Ottolenghi;M. Sheves;C. M. Einterz;S. Hug;J. W. Lewis;D. Kliger
用室温、纳秒激光光解和低温辐照研究了含有顺式-5，6-二氢-9-顺式视网膜发色团的人工牛视紫质色素顺-5，6-二氢异视紫红质(cis-5，6-dih-isorho，波长max 461 nm)的光解中间体。根据Yoshizawa和他的同事在T.Yoshizawa，T.，Y.Shichida和S.Matuoka的低温实验讨论了这些观察结果。1984年。视觉研究24：1455-1463)，以及与天然牛视紫红质(RHO)的光解中间体有关。结果表明，在5，6-DIH-ISORHO中，一种类似于天然视紫红质中间体(Batho)的初级底视紫质中间体迅速转化为蓝移中间体(BSI，最大波长430 nm)，这是天然视紫红质光解后不能观察到的。从光视紫红质(LUMI)到Meta-II视紫红质(META-II)的类似物是在BSI之后产生的，类似于它们在天然色素中由Batho产生。5，6-dih-isorho的底紫红质阶段的视网膜生色团被认为是通过对视网膜的几何重排来减轻由初级顺式异构化为反式异构化引起的应变。由于环与蛋白质的相互作用，这种导致BSI的重排不会在天然色素中如此迅速地发生。在天然色素中，Batho中的菌株只有在更长的时间尺度上才能得到缓解，其过程的速度由蛋白质松弛决定。
The photolysis intermediates of an artificial bovine rhodopsin pigment, cis-5,6-dihydro-isorhodopsin (cis-5,6,-diH-ISORHO, lambda max 461 nm), which contains a cis-5,6-dihydro-9-cis-retinal chromophore, are investigated by room temperature, nanosecond laser photolysis, and low temperature irradiation studies. The observations are discussed both in terms of low temperature experiments of Yoshizawa and co-workers on trans-5,6-diH-ISORHO (Yoshizawa, T., Y. Shichida, and S. Matuoka. 1984. Vision Res. 24: 1455–1463), and in relation to the photolysis intermediates of native bovine rhodopsin (RHO). It is suggested that in 5,6-diH-ISORHO, a primary bathorhodopsin intermediate analogous to the bathorhodopsin intermediate (BATHO) of the native pigment, rapidly converts to a blue-shifted intermediate (BSI, lambda max 430 nm) which is not observed after photolysis of native rhodopsin. The analogs from lumirhodopsin (LUMI) to meta-II rhodopsin (META-II) are generated subsequent to BSI, similar to their generation from BATHO in the native pigment. It is proposed that the retinal chromophore in the bathorhodopsin stage of 5,6-diH-ISORHO is relieved of strain induced by the primary cis to trans isomerization by undergoing a geometrical rearrangement of the retinal. Such a rearrangement, which leads to BSI, would not take place so rapidly in the native pigment due to ring-protein interactions. In the native pigment, the strain in BATHO would be relieved only on a longer time scale, via a process with a rate determined by protein relaxation.