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  1. 理学部(理工学研究科)
  2. 雑誌掲載論文

Calcium ions are required for the enhanced thermal stability of the light-harvesting-reaction center core complex from thermophilic purple sulfur bacterium Thermochromatium tepidum

https://doi.org/10.34405/00010244
https://doi.org/10.34405/00010244
36199fa9-120c-49a7-9f48-4fe746c1ba02
名前 / ファイル ライセンス アクション
20100095.pdf 20100095.pdf (737.9 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2010-07-02
タイトル
タイトル Calcium ions are required for the enhanced thermal stability of the light-harvesting-reaction center core complex from thermophilic purple sulfur bacterium Thermochromatium tepidum
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
ID登録
ID登録 10.34405/00010244
ID登録タイプ JaLC
Title in Japanese
Calcium ions are required for the enhanced thermal stability of the light-harvesting-reaction center core complex from thermophilic purple sulfur bacterium Thermochromatium tepidum
著者 KIMURA, Yukihiro / YU, Long Jiang / HIRANO, Yu / SUZUKI, Hiroaki / WANG, Zheng Yu

× KIMURA, Yukihiro / YU, Long Jiang / HIRANO, Yu / SUZUKI, Hiroaki / WANG, Zheng Yu

KIMURA, Yukihiro / YU, Long Jiang / HIRANO, Yu / SUZUKI, Hiroaki / WANG, Zheng Yu

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内容記述
内容記述タイプ Other
内容記述 Thermochromatium (Tch.) tepidum is a
thermophilic purple sulfur photosynthetic
bacterium collected from the Mammoth Hot
Springs, Yellowstone National Park. A
previous study showed that the lightharvesting-
reaction center core complex (LH1-
RC) purified from this bacterium is highly
stable at room temperature [Suzuki et al.,
(2007) Biochim. Biophys. Acta 1767, 1057-1063].
In this work, we demonstrate that thermal
stability of the Tch. tepidum LH1-RC is much
higher than that of its mesophilic counterparts
and the enhanced thermal stability requires
Ca2+ as a cofactor. Removal of the Ca2+ from
Tch. tepidum LH1-RC resulted in a complex
with the same degree of thermal stability to
that of the LH1-RCs purified from mesophilic
bacteria. The enhanced thermal stability can
be restored by addition of Ca2+ to the Ca2+-
depleted LH1-RC, and this process is fully
reversible. Interchange of the thermal
stability between the two forms is accompanied
by a shift of the LH1 Qy transition between 915
nm for the native and 880 nm for the Ca2+-
depleted LH1-RC. Differential scanning
calorimetry measurements reveal that
degradation temperature of the native LH1-RC
is 15 °C higher and the enthalpy change is
about 28% larger than the Ca2+-depleted LH1-
RC. Substitution of the Ca2+ with other metal
cations caused a decrease in thermal stability of
extent depending on the properties of the
cations. These results indicate that Ca2+ ions
play a dual role in stabilizing the structure of
the pigment-membrane protein complex and
altering its spectroscopic properties, and hence
provide insight into the adaptive strategy of
this photosynthetic organism to survive in
extreme environments using natural resources.
書誌情報 The Journal of Biological Chemistry

号 284, p. 93-99, 発行日 2009-01-02
フォーマット
内容記述タイプ Other
内容記述 application/pdf
著者版フラグ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
出版者
出版者 American Society for Biochemistry and Molecular Biology
資源タイプ
内容記述タイプ Other
内容記述 論文(Article)
資源タイプ・NII
Journal Article
資源タイプ・DCMI
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