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

Yasushi Imamoto, Hideki Kandori, Toshiyuki Okano, Yoshitaka Fukada, Yoshinori Shichida, Tôru Yoshizawa

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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 spectrophotometry. Irradiation of the iodopsin preparation at -185 °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., & Wald, G. (1967) Nature 214, 566-571] in which iodopsin was extracted with 2% digitonin. Therefore, photochemical and subsequent thermal behaviors of iodopsin were independent of the detergent to solubilize iodopsin. Irradiation of TV-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 iodopsin 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.

Original languageEnglish
Pages (from-to)9412-9416
Number of pages5
JournalBiochemistry®
Issue number24
Publication statusPublished - 1989
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Imamoto, Y., Kandori, H., Okano, T., Fukada, Y., Shichida, Y., & Yoshizawa, T. (1989). Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature. Biochemistry®, (24), 9412-9416.