Light-sensitive, purple-red organic pigment contained in the rod cells of the retina that allows the eye to see in black and white in dim light. It is composed of opsin, a protein, linked to retinal, a conjugated molecule (see conjugation) formed from vitamin A. Photons of light that enter the eye are absorbed by retinal and cause it to change its configuration, starting a biochemical chain of events that ends with impulses being sent along the optic nerve to the brain. In bright light, to protect rod cells from overstimulation, rhodopsin breaks down into retinal and opsin, both of which are colourless. In dim light or darkness the process is reversed (dark adaptation), and purple-red rhodopsin is reformed. Similar light-sensitive compounds made of retinal and other opsin proteins are the pigments in the retina's cone cells responsible for colour vision in bright light.
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Rhodopsin of the rods most strongly absorbs green-blue light and therefore appears reddish-purple, which is why it is also called "visual purple". It is responsible for monochromatic vision in the dark.
Several closely related opsins, the photopsins, exist that differ only in a few amino acids and in the wavelengths of light that they absorb most strongly. These pigments are found in the different types of the cone cells of the retina and are the basis of color vision. Humans have three different other opsins beside rhodopsin, with absorption maxima for yellowish-green (photopsin I), green (photopsin II), and bluish-violet (photopsin III) light.
The photoisomerization of rhodopsin has been studied in detail via x-ray crystallography on rhodopsin crystals. A first photoproduct called photorhodopsin forms within 200 femtoseconds after irradiation followed within picoseconds by a second one called bathorhodopsin with distorted all-trans bonds. This intermediate can be trapped and studied at cryogenic temperatures. Several models (e.g. the bicycle-pedal mechanism, hula-twist mechanism) attempt to explain how the retinal group can change its conformation without clashing with the enveloping rhodopsin protein pocket.
Mutation of the rhodopsin gene is a major contributor to various retinopathies such as retinitis pigmentosa. The disease-causing protein generally aggregates with ubiquitin in inclusion bodies, disrupts the intermediate filament network and impairs the ability of the cell to degrade non-functioning proteins which leads to photoreceptor apoptosis. Other mutations on rhodopsin lead to X-linked congenital stationary night blindness, mainly due to constitutive activation, when the mutations occur around the chromophore binding pocket of rhodopsin. Several other pathological states relating to rhodopsin have been discovered including poor post-Golgi trafficking, dysregulative activation, rod outer segment instability and arrestin binding.
Some prokaryotes express proton pumps called bacteriorhodopsin, proteorhodopsin, xanthorhodopsin to carry out phototrophy. Like rhodopsin, these contain retinal and have seven transmembrane alpha helices; however they are not coupled to a G protein. Bacterial halorhodopsin is a light-activated chloride pump. Finally, an alga is known to have an opsin that contains its own monolithic light-gated ion channel, channelrhodopsin. While bacteriorhodopsin, halorhodopsin, and channelrhodopsin all have significant sequence homology to one another, they have no detectable sequence identity to G-protein coupled receptor (GPCR) family where rhodopsins belong. Nevertheless, bacterial rhodopsins and GPCR are possibly evolutionary related, based on similarity of their three-dimensional structures. Therefore, they have been assigned to the same superfamily in Structural Classification of Proteins.
Phosphatidylethanolamine Enhances Rhodopsin Photoactivation and Transducin Binding in a Solid Supported Lipid Bilayer as Determined Using Plasmon-Waveguide Resonance Spectroscopy
Jan 01, 2005; ABSTRACT Flash photolysis studies have shown that the membrane lipid environment strongly influences the ability of...