Evidence for conformeric states of rhodopsin

Biophys Struct Mech. 1977 Apr 21;3(1):19-29. doi: 10.1007/BF00536450.

Abstract

Spectrophotometric measurements of metarhodopsin II appearance are made on five different kinds of rhodopsin preparations. Although the preparations differ greatly in their rhodopsin: phospholipid ratio, the meta II kinetics in all of them are strikingly similar in certain respects. Meta II appearance kinetics in all of the preparations are best described by two and only two exponentials. The ratio of these two rates is always about 5. The fast fraction: slow fraction ratio depends upon temperature. These fractions are reversibly convertible in the dark, and are interconverted on a time-scale which is long compared to the meta II appearance rate. It is shown that the kinetics of the earlier step in the bleaching sequence, viz., lumi-leads to meta I, is also described by double exponentials. Again the ratio of rates is ca. 5 and the fast-slow fractions correspond to those found in the meta I leads to meta II step. It is proposed that these facts support an hypothesis for the existence of two conformeric states of rhodopsin which are in thermal equilibrium. Thermodynamic parameters associated with this proposed equilibrium are presented.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Protein Conformation
  • Retinal Pigments*
  • Rhodopsin*

Substances

  • Retinal Pigments
  • Rhodopsin