Rhodopsin
Title: Rhodopsin
CAS Registry Number: 9009-81-8
Additional Names: Visual purple
Literature References: Mol wt ~40,000. A photoreceptor protein found in the rods of the retina of the eye. Composed of 11-cis retinal, q.v., bound as a protonated Schiff base to a lysine moiety in the apoprotein opsin, q.v. Prepn from retinal and opsin: G. Wald, P. K. Brown, Proc. Natl. Acad. Sci. USA 36, 84 (1950); R. Hubbard, G. Wald, ibid. 37, 69 (1951). Purification and amino acid compn of bovine rhodopsin: Shields et al., Biochim. Biophys. Acta 147, 238 (1967). Synthesis of labelled rhodopsin and studies on the active site: Hirtenstein, Akhtar, Biochem. J. 119, 359 (1970). Characterization in synthetic membranes: W. L. Hubbell, Acc. Chem. Res. 8, 85 (1975). Amino acid sequence of bovine rhodopsin: P. A. Hargrave et al., Biophys. Struct. Mech. 9, 235 (1983). Studies on transmembrane molecular structure: E. A. Dratz, P. A. Hargrave, Trends Biochem. Sci. 8, 128 (1983). Crystal structure: K. Palczewski et al., Science 289, 739 (2000). Isoln and sequence of gene encoding bovine rhodopsin: J. Nathans, D. S. Hogness, Cell 34, 807 (1983); of gene encoding human rhodopsin: eidem, Proc. Natl. Acad. Sci. USA 81, 4851 (1984). Exposure to light initiates the conversion of rhodopsin through a series of distinct intermediates to yield opsin + trans-retinal: R. Hubbard, A. Kropf, ibid. 44, 130 (1958); R. Hubbard et al., Nature 183, 142 (1959); B. Honig et al., Proc. Natl. Acad. Sci. USA 76, 2503 (1979). Review of visual transduction and bioregulation of absorption maxima: K. Nakanishi, Pure Appl. Chem. 57, 769-776 (1985). Reviews: T. G. Ebrey, B. Honig, Q. Rev. Biophys. 8, 129-184 (1975); D. F. O'Brien, Science 218, 961-966 (1982); A. Maeda, T. Yoshizawa, Photochem. Photobiol. 35, 891-898 (1982); P. S. Zurer, Chem. Eng. News 61, 24-35 (Nov. 28, 1983). See also: Methods Enzymol. 81 and 88, Lester Packer, Ed. (Academic Press, New York, 1982).

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