一种在无脊椎动物眼睛视觉循环中催化11-顺式视黄醛形成的蛋白质的结构。

Structure of a protein catalyzing the formation of 11 cis-retinal in the visual cycle of invertebrate eyes.

作者信息

Pepe I M, Cugnoli C, Peluso M, Vergani L, Boero A

出版信息

Cell Biophys. 1987 Feb;10(1):15-22. doi: 10.1007/BF02797070.

Abstract

A pigment made up of a protein able to bind retinal as well as retinol is described. The molecule consists of a dimer with a molecular weight of 50,000 which binds one molecule of retinal. The binding site for retinal is a Schiff base buried in the interior of the protein. Retinol is probably bound to the protein in the same site as for retinal, although not covalently, as suggested by the absorbance spectra. The protein, extracted from honeybee retina, is involved in visual pigment metabolism, and its structure may elucidate the mechanism of the stereospecific photoisomerization of all trans-retinal to 11-cis-retinal.

摘要

描述了一种由能够结合视黄醛以及视黄醇的蛋白质组成的色素。该分子由分子量为50,000的二聚体组成，可结合一分子视黄醛。视黄醛的结合位点是埋在蛋白质内部的席夫碱。如吸收光谱所示，视黄醇可能与视黄醛结合在蛋白质的同一部位，尽管不是共价结合。从蜜蜂视网膜中提取的这种蛋白质参与视觉色素代谢，其结构可能阐明全反式视黄醛立体定向光异构化为11-顺式视黄醛的机制。