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Chromophore Protein Interactions in Visual Pigments and their Analogs

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Environmental Effects on Molecular Structure and Properties

Part of the book series: The Jerusalem Symposia on Quantum Chemistry and Biochemistry ((JSQC,volume 8))

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Abstract

Visual pigments consist of a chromophore, 11-cis retinal, or 3-dehydroretinal, co-valently bound to a protein called an opsin [1]. The covalent bond involves a Schiff base between the terminal carbon in the polyene chain and the ε-amino group of one of the lysines in the protein. Visual pigments have a number of functions. Their primary role is to absorb light and then propagate the visual response but they may also be involved in other aspects of photoreceptor cell function [2]. It is generally accepted that the only action of light on the pigment is to photoisomerize the 11-cis chromophore to its all trans conformation which then leaves the protein in a series of dark reactions. As a result of this process the pigments lose their color since retinal isomers absorb in the ultraviolet (ca 370 nm). It appears then that there is a very specific chromophore-protein interaction which is responsible for the appearance of color upon pigment formation.

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© 1976 D. Reidel Publishing Company, Dordrecht-Holland

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Honig, B., Greenberg, A.D. (1976). Chromophore Protein Interactions in Visual Pigments and their Analogs. In: Pullman, B. (eds) Environmental Effects on Molecular Structure and Properties. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 8. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-1837-1_21

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  • DOI: https://doi.org/10.1007/978-94-010-1837-1_21

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-1839-5

  • Online ISBN: 978-94-010-1837-1

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