A Model of the Light Dependent Regulation of Retinal Rod Phosphodiesterase, Guanylate Cyclase and the Cation Flux

  • M. W. Bitensky
  • D. Torney
  • A. Yamazaki
  • M. M. Whalen
  • J. S. George
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 221)


In the 1880’s Kuhn dissected dark adapted eyes and observed that the retina’s red/purple “visual pigment”, changed rapidly to a pale yellow upon illumination. Years later, George Wald and Ruth Hubbard chemically characterized the rod visual pigment as consisting of opsin and 11-cis retinal (Wald, 1968). They demonstrated that the photoisomerization of rhodopsin was driven by a photon induced change in the configuration of 11-cis retinal (to all-trans), which was accompanied by conformational changes in the protein opsin. Subsequently, Wald, Yoshizawa and others were able to identify a series of spectral intermediates that appeared in rapid succession following the illumination of rhodopsin. The early intermediates could only be captured by stabilization at low temperatures or ultrafast spectroscopy. The major opsin photoconformers are called batho, hypso, meta I, meta II and meta III rhodopsin (Wald 1968; Birge, 1981). The meta II conformation was subsequently found to be enzymatically active (see below).


Outer Segment Guanylate Cyclase Light Response Disk Membrane Guanylate Cyclase Activity 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • M. W. Bitensky
    • 1
  • D. Torney
    • 1
  • A. Yamazaki
    • 1
  • M. M. Whalen
    • 1
  • J. S. George
    • 1
  1. 1.Los Alamos National LaboratoryLos AlamosUSA

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