Azuma K, Azuma M, Suzuki T
Biochim Biophys Acta. 1975 Jun 26;393(2):520-30. doi: 10.1016/0005-2795(75)90079-3.
In the bleaching process of cephalopod rhodopsin, a new intermediate was found in the conversion process from lumirhodopsin to metarhodopsin. This intermediate of octopus has an absorption peak at about 475 nm and has been named as M475. The circular dichroism value of M475 is too small to be evaluated. On the other hand, lumirhodopsin shows a negative CD at 470 nm, a positive CD at 350 nm and a large positive CD band with three peaks at 280, 287 and 295 nm. Such a large CD band in the ultraviolet region is not observed in rhodopsin, M475 and metarhodopsin. This CD seems to be mainly due to tryptophan and tyrosine residues restricted in free rotation in the protein moiety of lumirhodopsin. The intermediate in the photoregeneration process of cephalopod rhodopsin, P380, has a positive CD band at the main peak, 380 nm, and also a large positive CD band in the ultraviolet region like lumirhodopsin.
在头足类视紫红质的漂白过程中,在从发光视紫红质向变视紫红质的转化过程中发现了一种新的中间体。这种章鱼的中间体在约475nm处有一个吸收峰,并被命名为M475。M475的圆二色性值太小,无法评估。另一方面,发光视紫红质在470nm处显示负的圆二色性,在350nm处显示正的圆二色性,并且在280、287和295nm处有一个带有三个峰的大的正圆二色性带。在视紫红质、M475和变视紫红质中未观察到在紫外区域有如此大的圆二色性带。这种圆二色性似乎主要归因于发光视紫红质蛋白质部分中自由旋转受限的色氨酸和酪氨酸残基。头足类视紫红质光再生过程中的中间体P380在主峰380nm处有一个正的圆二色性带,并且像发光视紫红质一样在紫外区域也有一个大的正圆二色性带。