Breaking the covalent bond - A pigment property that contributes to desensitization in cones

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Abstract

Retinal rod and cone pigments consist of an apoprotein, opsin, covalently linked to a chromophore, 11-cis retinal. Here we demonstrate that the formation of the covalent bond between opsin and 11-cis retinal is reversible in darkness in amphibian red cones, but essentially irreversible in red rods. This dissociation, apparently a general property of cone pigments, results in a surprisingly large amount of free opsin - about 10% of total opsin - in dark-adapted red cones. We attribute this significant level of free opsin to the low concentration of intracellular free 11-cis retinal, estimated to be only a tiny fraction (∼0.1 %) of the pigment content in red cones. With its constitutive transducin-stimulating activity, the free cone opsin produces an ∼2-fold desensitization in red cones, equivalent to that produced by a steady light causing 500 photoisomerizations s-1. Cone pigment dissociation therefore contributes to the sensitivity difference between rods and cones. Copyright ©2005 by Elsevier Inc.

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Kefalov, V. J., Estevez, M. E., Kono, M., Goletz, P. W., Crouch, R. K., Cornwall, M. C., & Yau, K. W. (2005). Breaking the covalent bond - A pigment property that contributes to desensitization in cones. Neuron, 46(6), 879–890. https://doi.org/10.1016/j.neuron.2005.05.009

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