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Neuron. 2005 Jun 16;46(6):879-90.

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

Author information

1
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. vkefalov@jhmi.edu

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 (approximately 0.1 %) of the pigment content in red cones. With its constitutive transducin-stimulating activity, the free cone opsin produces an approximately 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.

PMID:
15953417
PMCID:
PMC2885911
DOI:
10.1016/j.neuron.2005.05.009
[Indexed for MEDLINE]
Free PMC Article

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