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Activation of visual pigment: Chormophore structure and function

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons84015

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

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Zitation

Kirschfeld, K. (1986). Activation of visual pigment: Chormophore structure and function. In The Molecular Mechanism of Photoreception (pp. 31-49). Berlin, Germany: Springer.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0013-EFED-C
Zusammenfassung
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.