Activation of visual pigment: Chormophore structure and function

Kirschfeld, K

doi:10.1007/978-3-642-70444-4_3

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Activation of visual pigment: Chormophore structure and function

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Kirschfeld, K
Former Department Comparative Neurobiology, Max Planck Institute for Biological Cybernetics, Max Planck Society;
Max Planck Institute for Biological Cybernetics, Max Planck Society;

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Citation

Kirschfeld, K. (1986). Activation of visual pigment: Chormophore structure and function. In H. Stieve (Ed.), The Molecular Mechanism of Photoreception: Report of the Dahlem Workshop on the Molecular Mechanism of Photoreception Berlin 1984, November 25–30 (pp. 31-49). Berlin, Germany: Springer.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0013-EFED-C

Abstract

Besides the “classical” chromophores retinal (visual pigment: rhodopsin) and 3-dehydroretinal (visual pigment: porphyropsin), recently a new chromophore has been found in several insect groups: 3-hydroxyretinal (visual pigment: xanthopsin). Evolutionary aspects are considered — the first interaction of light with the photoreceptor must not necessarily take place at the Schiff base-linked chromophore. In many photoreceptors, e.g., of many fly species, light can be absorbed by a sensitizing pigment which then transfers energy (Förster mechanism) to the Schiff base-linked chromophore. This chromophore is then isomerized and leads to excitation of the receptor. The sensitizing pigment in higher flies is identified as 3-hydroxyretinol, and in one more primitive fly species (Simuliid) most likely as retinol. Functional consequences of sensitization are illustrated.