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Spectral Tuning of Shortwave‐sensitive Visual Pigments in Vertebrates †
Author(s) -
Hunt David M.,
Carvalho Lívia S.,
Cowing Jill A.,
Parry Juliet W. L.,
Wilkie Susan E.,
Davies Wayne L.,
Bowmaker James K.
Publication year - 2007
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1562/2006-06-27-ir-952
Subject(s) - rhodopsin , pigment , opsin , visual pigments , protonation , context (archaeology) , biology , ultraviolet , phylogenetic tree , retinal pigments , vertebrate , chemistry , botany , ion , genetics , retinal , physics , optics , paleontology , organic chemistry , gene
Of the four classes of vertebrate cone visual pigments, the shortwave‐sensitive SWS1 class shows some of the largest shifts in λ max , with values ranging in different species from 390–435 nm in the violet region of the spectrum to <360 nm in the ultraviolet. Phylogenetic evidence indicates that the ancestral pigment most probably had a λ max in the UV and that shifts between violet and UV have occurred many times during evolution. In violet‐sensitive (VS) pigments, the Schiff base is protonated whereas in UV‐sensitive (UVS) pigments, it is almost certainly unprotonated. The generation of VS pigments in amphibia, birds and mammals from ancestral UVS pigments must involve therefore the stabilization of protonation. Similarly, stabilization must be lost in the evolution of avian UVS pigments from a VS ancestral pigment. The key residues in the opsin protein for these shifts are at sites 86 and 90, both adjacent to the Schiff base and the counterion at Glu113. In this review, the various molecular mechanisms for the UV and violet shifts in the different vertebrate groups are presented and the changes in the opsin protein that are responsible for the spectral shifts are discussed in the context of the structural model of bovine rhodopsin.