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  • Title: Two forms of intermediates of frog rhodopsin in rod outer segments.
    Author: Sasaki N, Tokunaga F, Yoshizawa T.
    Journal: Biochim Biophys Acta; 1983 Jan 13; 722(1):80-7. PubMed ID: 6600624.
    Abstract:
    Using frog rod outer segments, we measured changes of the absorption spectrum during the conversion of rhodopsin to a photosteady-state mixture composed of rhodopsin, isorhodopsin and bathorhodopsin by irradiation with blue light (440 nm) at -190 degrees C and during the reversion of bathorhodopsin to a mixture of rhodopsin and isorhodopsin by irradiation with red light (718 nm) at -190 degrees C. The reaction kinetics was expressed by one exponential in the former case and by two exponentials in the latter. These results suggest that rhodopsin is composed of a single molecular species, while bathorhodopsin is composed of two kinds of molecular species designated as batho1-rhodopsin and batho2-rhodopsin. On warming the two forms of bathorhodopsin, each bathorhodopsin converted to its own lumirhodopsin, metarhodopsin I and finally a free all-trans-retinal plus opsin. The absorption spectra of the two forms of bathorhodopsin, lumirhodopsin and metarhodopsin I were measured at -190 degrees C. We infer that a rhodopsin molecule in the excited state relaxes to either batho1-rhodopsin or batho2-rhodopsin, and then converts to its own intermediates through one of the two parallel pathways.
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