論文

査読有り
2003年11月

Effect of anion binding on the thermal reverse reaction of bathoiodopsin: Anion stabilizes two forms of iodopsin

BIOCHEMISTRY
  • T Hirano
  • ,
  • H Imai
  • ,
  • Y Shichida

42
43
開始ページ
12700
終了ページ
12707
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/bi034671w
出版者・発行元
AMER CHEMICAL SOC

The thermal reactions of the bathoproduct of the long wavelength sensitive visual pigment iodopsin were investigated under various anionic and environmental conditions, to get an insight into the mechanism leading to the unusual thermal isomerization of the retinal chromophore from the trans to the 11-cis form at very low temperatures (-160 degreesC). The all-trans chromophore of the bathoiodopsin produced from iodopsin in the presence of chloride thermally reverted to the 11-cis form, while in the presence of nitrate it kept its all-trans configuration upon warming. Different protein environments, either in a detergent or in phosphatidylcholine (PC) liposomes, did not change the reaction characteristics of the bathoiodopsins under the two anionic conditions. However, reaction characteristics of bathoiodopsins produced in the absence of small anions were dependent on the environment. The trans-to-cis isomerization occurred upon warming of bathoiodopsin in the presence of detergent but not in liposomes. Spectral measurements revealed that iodopsin in the absence of small anions is a mixture of two spectrally distinct forms that exhibit absorption maxima and reaction characteristics similar to those of chloride-bound and nitrate-bound iodopsins, respectively. Thus, iodopsin exhibits two conformational states, each of which is stabilized by the binding of chloride and nitrate, respectively.

リンク情報
DOI
https://doi.org/10.1021/bi034671w
J-GLOBAL
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902285366042659
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/14580218
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000186531100031&DestApp=WOS_CPL
ID情報
  • DOI : 10.1021/bi034671w
  • ISSN : 0006-2960
  • J-Global ID : 200902285366042659
  • PubMed ID : 14580218
  • Web of Science ID : WOS:000186531100031

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