OSA's Digital Library

Journal of the Optical Society of America

Journal of the Optical Society of America

  • Vol. 41, Iss. 12 — Dec. 1, 1951
  • pp: 949–955

The Photochemical Basis of Rod Vision

GEORGE WALD  »View Author Affiliations

JOSA, Vol. 41, Issue 12, pp. 949-955 (1951)

View Full Text Article

Acrobat PDF (802 KB)

Browse Journals / Lookup Meetings

Browse by Journal and Year


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools



The photochemical system upon which the excitation of rod vision depends has been analyzed, and all its component processes brought into free solution. The only action of light in this system is to convert rhodopsin to the highly unstable lumi-rhodopsin. This bleaches in the dark via the intermediate meta-rhodopsin to a mixture of the carotenoid, retinene1, and the colorless protein, opsin. Retinene1 is reduced to vitamin A1 by the coenzyme, reduced cozymase, acting in concert with the enzyme retinene reductase or alcohol dehydrogenase. These are the degradative processes in the rhodopsin system.

The resynthesis of rhodopsin from these products is the basis of dark adaptation. A mixture of opsin and retinene1, forms rhodopsin spontaneously in the dark. The retinene reductase system, left to itself, reduces retinene1 to vitamin A1. In the presence of opsin, however, it oxidizes vitamin A1 to retinene1 as rapidly as retinene, condenses with opsin to form rhodopsin.

A mixture of four substances in solution performs all the reactions of the rhodopsin system: vitamin A1, cozymase, alcohol dehydrogenase, and opsin. Opsin is the only one of these specific to the retina.

The synthesis of rhodopsin requires the presence of free sulfhydryl (-SH) groups in opsin. Conversely when rhodopsin bleaches, two such groups are liberated for each retinene1 formed. Based upon these changes, an artificial system has been devised in which the bleaching of rhodopsin results in an electrical variation. This may provide a model for the excitation process in rod vision.

GEORGE WALD, "The Photochemical Basis of Rod Vision," J. Opt. Soc. Am. 41, 949-955 (1951)

Sort:  Author  |  Journal  |  Reset


  1. G. Wald, Documenta Ophth. 3, 94 (1949a).
  2. G. Wald, J. Gen. Physiol. 19, 351 (1935–36) 21, 795 (1937–38).
  3. G. Wald and A.-B. Clark, J. Gen. Physiol. 21, 93 (1937–38).
  4. H. K. Hartline and P. R. McDonald, J. Cellular Comp. Physiol. 30, 225 (1947).
  5. R. C. C. St. George and G. Wald, Biol. Bull. 97, 248 (1949).
  6. G. Wald, Harvey Lectures 41, 117 (1945–46).
  7. Wald, Durell, and St. George, Science 111, 179 (1950).
  8. Ball, Goodwin, and Morton, Biochem. J. 42, 516 (1948).
  9. G. Wald and R. Hubbard, J. Gen. Physiol. 32, 367 (1948–1949).
  10. G. Wald, J. Gen. Physiol. 31, 489 (1947–1948).
  11. G. Wald, Science 109, 482 (1949); Biochim. et Biophys. Acta 4, 215 (1950a).
  12. A. F. Bliss, Biol. Bull. 97, 221 (1949).
  13. R. Hubbard and G. Wald, Proc. Nat. Acad. Sci. 37, 69 (1951).
  14. Hecht, Chase, Shlaer, and Haig, Science 84, 331 (1936).
  15. A. M. Chase and E. L. Smith, J. Gen. Physiol. 23, 21 (1939–1940).
  16. G. Wald and P. K. Brown, Proc. Nat. Acad. Sci. 36, 84 (1950).
  17. G. Wald and R. Hubbard, Proc. Nat. Acad. Sci. 36, 92 (1950).
  18. This is not its only function. The pigment epithelium contains also water-soluble, heat-labile factors, apparently protein, which aid the synthesis of rhodopsin (A. F. Bliss, Fed. Proc. 9, 12 (1950); reference 14). These have not yet been identified.
  19. G. Wald and P. K. Brown, Fed. Proc. 10, 266 (1951a). Also J. Gen. Physiol. to be published (1951–52). G. Wald and P. K. Brown, Science 113, 474 (1951b).
  20. I. M. Kolthoff and W. E. Harris, Ind. Eng. Chem., Anal. Ed. 18, 161 (1946).

Cited By

Alert me when this paper is cited

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited