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

Research output: Contribution to journalArticle

39 Citations (Scopus)

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

Fingerprint

Chlorides
Hot Temperature
Ions
Temperature
iodopsin
Irradiation
Digitonin
Spectrophotometry
Phosphatidylcholines
Detergents

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.

Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature. / Imamoto, Yasushi; Kandori, Hideki; Okano, Toshiyuki; Fukada, Yoshitaka; Shichida, Yoshinori; Yoshizawa, Tôru.

In: Biochemistry®, No. 24, 1989, p. 9412-9416.

Research output: Contribution to journalArticle

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®, no. 24, pp. 9412-9416.
Imamoto, Yasushi ; Kandori, Hideki ; Okano, Toshiyuki ; Fukada, Yoshitaka ; Shichida, Yoshinori ; Yoshizawa, Tôru. / Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature. In: Biochemistry®. 1989 ; No. 24. pp. 9412-9416.
@article{e4b9d5292a464ec9946bd569d94d2a43,
title = "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 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.",
author = "Yasushi Imamoto and Hideki Kandori and Toshiyuki Okano and Yoshitaka Fukada and Yoshinori Shichida and T{\^o}ru Yoshizawa",
year = "1989",
language = "English",
pages = "9412--9416",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "24",

}

TY - JOUR

T1 - Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature

AU - Imamoto, Yasushi

AU - Kandori, Hideki

AU - Okano, Toshiyuki

AU - Fukada, Yoshitaka

AU - Shichida, Yoshinori

AU - Yoshizawa, Tôru

PY - 1989

Y1 - 1989

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0024350856&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024350856&partnerID=8YFLogxK

M3 - Article

SP - 9412

EP - 9416

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 24

ER -