Abstract
THE vertebrate visual pigment, rhodopsin, is located in the outer segment disks of the rod photoreceptor cells, and consists of a chromophore, 11-cis retinal, bound to a protein, opsin. During light adaptation, 11-cis retinal is isomerised to the all-trans configuration. All-trans retinal is then reduced to retinol by an oxido-reductase in the rod outer segments1–4, and retinol diffuses to areas adjacent to the rod outer segments, where it is esterified to form retinyl esters5–12. During dark adaptation rhodopsin is regenerated as essentially the reverse processes occur; however, it is not known in what form (retinyl ester, retinol, retinal) the chromophoric group is re-isomerised to the 11-cis configuration.
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ZIMMERMAN, W., YOST, M. & DAEMEN, F. Dynamics and function of vitamin A compounds in rat retina after a small bleach of rhodopsin. Nature 250, 66–67 (1974). https://doi.org/10.1038/250066a0
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DOI: https://doi.org/10.1038/250066a0
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