The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Tautomeric Forms of Metarhodopsin
Open accessAbstract
Light isomerizes the chromophore of rhodopsin, 11-cis retinal (formerly retinene), to the all-trans configuration. This introduces a succession of unstable intermediates—pre-lumirhodopsin, lumirhodopsin, metarhodopsin —in which all-trans retinal is still attached to the chromophoric site on opsin. Finally, retinal is hydrolyzed from opsin. The present experiments show that metarhodopsin exists in two tautomeric forms, metarhodopsins I and II, with λmax 478 and 380 mµ. Metarhodopsin I appears first, then enters into equilibrium with metarhodopsin II. In this equilibrium, the proportion of metarhodopsin II is favored by higher temperature or pH, neutral salts, and glycerol. The change from metarhodopsin I to II involves the binding of a proton by a group with pK 6.4 (imidazole?), and a large increase of entropy. Metarhodopsin II has been confused earlier with the final mixture of all-trans retinal and opsin (λmax 387 mµ), which it resembles in spectrum. These two products are, however, readily distinguished experimentally.
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Citations
Cites
Pre-Lumirhodopsin and the Bleaching of Visual Pigments
YOSHIZAWA, T., & WALD, G. (1963) · Nature · doi:10.1038/1971279a0 · Cited by 520
Self-citationTHE RHODOPSIN SYSTEM OF THE SQUID
Hubbard, R., & St. George, R. C. C. (1958) · The Journal of General Physiology · doi:10.1085/jgp.41.3.501 · Cited by 315
Self-citationDartnall, H. J. A. (1958) · AIBS Bulletin · doi:10.2307/1292183 · Cited by 305
THE ACTION OF LIGHT ON RHODOPSIN
Hubbard, R., & Kropf, A. (1958) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.44.2.130 · Cited by 301
Self-citationTHE MECHANISM OF BLEACHING RHODOPSIN
Kropf, A., & Hubbard, R. (1958) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1958.tb39550.x · Cited by 239
Self-citationTHE ROLE OF SULFHYDRYL GROUPS IN THE BLEACHING AND SYNTHESIS OF RHODOPSIN
Wald, G., & Brown, P. K. (1952) · Journal of General Physiology · doi:10.1085/jgp.35.5.797 · Cited by 210
Self-citationThe Light Reaction in the Bleaching of Rhodopsin
Wald, G., Durell, J., & St. George, R. C. C. (1950) · Science · doi:10.1126/science.111.2877.179 · Cited by 183
Self-citationStudies on rhodopsin. 9. pH and the hydrolysis of indicator yellow
Morton, R. A., & Pitt, G. A. J. (1955) · Biochemical Journal · doi:10.1042/bj0590128 · Cited by 160
Visual Pigments of the Octopus and Cuttlefish
BROWN, P. K., & BROWN, P. S. (1958) · Nature · doi:10.1038/1821288a0 · Cited by 160
Self-citationTHE THERMAL STABILITY OF RHODOPSIN AND OPSIN
Hubbard, R. (1958) · The Journal of General Physiology · doi:10.1085/jgp.42.2.259 · Cited by 133
Self-citation
Cited by
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
Chemistry and metabolism of lipids in the vertebrate retina
Fliesler, A. J., & Anderson, R. E. (1983) · Progress in Lipid Research · doi:10.1016/0163-7827(83)90004-8 · Cited by 1,052
Molecular Basis of Visual Excitation
Wald, G. (1968) · Science · doi:10.1126/science.162.3850.230 · Cited by 832
Self-citationThe Molecular Basis of Visual Excitation
WALD, G. (1968) · Nature · doi:10.1038/219800a0 · Cited by 824
Self-citationDark adaptation and the retinoid cycle of vision
Lamb, T. D., & Pugh, E. N. (2004) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2004.03.001 · Cited by 725
Metadata
- Authors
- Matthews, R. G., Hubbard, R., Brown, P. K., & Wald, G.
- Venue
- The Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 1963-11-01
- Volume
- 47
- Issue
- 2
- Pages
- 215-240
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- OpenAlex
- W2104782686
- Cited by
- 601
- References
- 19
- FWCI
- 6.24
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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