Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature

Abstract

The photochemical and the subsequent thermal behaviors of iodopsin (Cl-bound form) and N-iodopsin (iodopsin whose Cl- was replaced by NO3-) in CHAPS-phosphatidylcholine (PC) were studied by low-temperature spectrophotomery. Irradiation of the iodopsin preparation at -185.degree. C produced a photo-steady-state mixture composed of iodopsin, bathoiodopsin, and isoiodopsin. Bathoiodopsin was thermally reverted to the original iodopsin. These results were almost the same as those reported previously [Yoshizawa, T., and Wald, G. (1967) Nature 214, 556-571] in which iodopsin was extracted with 2% digitonin. Therefore, photochemical and subsequent thermal behaviors of iodopsin were independent of the detergent to solubilize iodopsin. Irradition of N-iodopsin at -185% C produced the similar photo-steady-state mixture. However, N-bathoiodopsin was thermally converted to the next intermediate, presumably N-lumiiodopsin. These results suggest that the batho-lumi transition of iodospin at low temperature is likely to be inhibited by the Cl- bound to the protein moiety of iodopsin, while at room temperature the Cl- bound to iodopsin could be released on the conversion process of batho- to lumiiodopsin.