|
Retinene, the isomer
![]() |
We now have the basis for understanding the chemical basis of vision.
Let's now take a closer look at how light and retinene interact. The diagram at left shows a retinene molecule with it's carbon atoms numbered. Notice the alternating single and double bonds that begin at carbon #5 and continue through #15. Referring to our description of cis and trans isomer, you may correctly recognize that there are many isomer possibilities amongst all these double bond pairs in this conjugated system. There is one pair of carbon atoms that is particular to vision This is the pair of carbons that form the double bond at 11 and 12. Wald discovered that the cis isomer at carbons 11 and 12 of retinene fits nicely into a point of attachment of the protein, opsin. This complex of retinene with opsin forms a rhodopsin. |
![]() |
The diagram at left illustrates the principals of light activation of retinene. The cis isomer is shaped in such a way that only it attaches to the opsin. This complex yeilds a pigment with a deep orange to violet pigment. There are many different opsins and the resultant pigment is dependant upon which we refer to.
A photon of light is absorbed by the pi electrons in the conjugated chain of the retinene. This higher energy level flips the cis isomer to the trans position, straightening out the molecule. The straightened trans-retinene no longer fits the opsin protein and comes away. The deeper colors of the original pigment is replaced by the yellow color of free retinene. This process is sometimes referred to as a "bleaching" of the visual pigments. It is this process or isomerization that forms the "trigger" that begins the events that lead to vision. It's the mechanism by which the energy contained in a quantum of the suns energy can be transferred to the biochemical world of our bodies. |
References used in the Vision sections of this site. Hartline., H.K., Wagner, H.G., Ratcliff, Floyd, Inhibition in the Eye of Limulus, Journal of General Physiology, 1956, 39:5 pp.651-673 Westerman, L.A., Barlow, R.B., Ultraviolet responses of the Limulus mediann ocellus, Biological Bulletin, 1981 161 352-353 Barlow, R.B., Ireland, C.I., Kass, L., Vision in Limulus mating behavior, Biological Bulletin, 1981 161 339-340 Powers, M.K., Barlow, R.B., Circadian changes in visual sensitivity of Limulus: behavioral evidence, Biological Bulletin, 1981 161 350-351 Hubbard, Ruth. Retinene Isomerase, Journal of General Physiology, Vol 39, No. 6 pp.935-962 Wald, G., Human Vision and the Spectrum, Science, 1945, 101, 653 Wald, G., Life and Light, Scientific American, Oct. 1959, pp 92-108 Invertebrate Photoreceptors, A Comparative Analysis, Jerome J. Wolken, Academic Press, NY, 1971 Kimbel, R.L., Poincelot, R.P., Abrahamson, E.W., Chromophore Transfer from Lipid to Protein in Bovine Rhodopsin, Biochemistry 1970 9:8 1817 Westerman, L.A, Barlow, R.B, Ultraviolet responses of the Limulus median ocellus, Biological Bulletin General Scientific Meetings. 161:3 352-353 Barlow, R.B, Ireland, L.C., Cass, L., Viision in Limulus mating behavior, Biological Bulletin General Scientific Meetings. 161:3 339-340 Sargent, William., The Year of the Crab., W.W. Norton & Company 1987