This paper is part of the Proceedings of the 12th International Conference on Retinal Proteins held at Awaji Island, Hyogo, Japan on 4–8 June 2006.
Spectral Tuning of Shortwave-sensitive Visual Pigments in Vertebrates†
Article first published online: 14 MAR 2007
Photochemistry and Photobiology
Volume 83, Issue 2, pages 303–310, March/April 2007
How to Cite
Hunt, D. M., Carvalho, L. S., Cowing, J. A., Parry, J. W. L., Wilkie, S. E., Davies, W. L. and Bowmaker, J. K. (2007), Spectral Tuning of Shortwave-sensitive Visual Pigments in Vertebrates. Photochemistry and Photobiology, 83: 303–310. doi: 10.1562/2006-06-27-IR-952
- Issue published online: 14 MAR 2007
- Article first published online: 14 MAR 2007
- Received 27 June 2006; accepted 11 September 2006; published online 21 September 2006; DOI: 10.1562/2006-06-27-IR-952
Of the four classes of vertebrate cone visual pigments, the shortwave-sensitive SWS1 class shows some of the largest shifts in λmax, 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 λmax 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.