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Constant Enthalpy Change Value during Pyrophosphate Hydrolysis within the Physiological Limits of NaCl

https://hiroshima.repo.nii.ac.jp/records/2007236
https://hiroshima.repo.nii.ac.jp/records/2007236
cf68a7e5-ddd6-4829-b80e-a4ea8a5bccce
名前 / ファイル ライセンス アクション
J. J. Biol. Chem_288_29247.pdf (1.1 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Constant Enthalpy Change Value during Pyrophosphate Hydrolysis within the Physiological Limits of NaCl
言語 en
作成者 Wakai, Satoshi

× Wakai, Satoshi

en Wakai, Satoshi

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Kidokoro, Shun-ichi

× Kidokoro, Shun-ichi

en Kidokoro, Shun-ichi

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Masaki, Kazuo

× Masaki, Kazuo

en Masaki, Kazuo

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Nakasone, Kaoru

× Nakasone, Kaoru

en Nakasone, Kaoru

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Sambongi, Yoshihiro

× Sambongi, Yoshihiro

en Sambongi, Yoshihiro

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 This research was originally published in the Journal of Biological Chemistry. Satoshi Wakai, Shun-ichi Kidokoro, Kazuo Masaki, Kaoru Nakasone, and Yoshihiro Sambongi. Constant Enthalpy Change Value during Pyrophosphate Hydrolysis within the Physiological Limits of NaCl. J Biol Chem. 2013; 288:29247-29251. © 2013 the American Society for Biochemistry and Molecular Biology, Inc.
内容記述
内容記述 A decrease in water activity was thought to result in smaller enthalpy change values during PPi hydrolysis, indicating the importance of solvation for the reaction. However, the physiological significance of this phenomenon is unknown. Here, we combined biochemistry and calorimetry to solve this problem using NaCl, a physiologically occurring water activity-reducing reagent. The pyrophosphatase activities of extremely halophilic Haloarcula japonica, which can grow at ∼4 m NaCl, and non-halophilic Escherichia coli and Saccharomyces cerevisiae were maximal at 2.0 and 0.1 m NaCl, respectively. Thus, halophilic and non-halophilic pyrophosphatases exhibit distinct maximal activities at different NaCl concentration ranges. Upon calorimetry, the same exothermic enthalpy change of −35 kJ/mol was obtained for the halophile and non-halophiles at 1.5–4.0 and 0.1–2.0 m NaCl, respectively. These results show that solvation changes caused by up to 4.0 m NaCl (water activity of ∼0.84) do not affect the enthalpy change in PPi hydrolysis. It has been postulated that PPi is an ATP analog, having a so-called high energy phosphate bond, and that the hydrolysis of both compounds is enthalpically driven. Therefore, our results indicate that the hydrolysis of high energy phosphate compounds, which are responsible for biological energy conversion, is enthalpically driven within the physiological limits of NaCl.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported by Grant-in-aid for Scientific Research on Innovative Areas 20118005 from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
出版者
出版者 The American Society for Biochemistry and Molecular Biology, Inc.
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
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1074/jbc.M113.502963
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.M113.502963
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0021-9258
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1083-351X
開始ページ
開始ページ 29247
書誌情報 Journal of Biological Chemistry
Journal of Biological Chemistry

巻 288, 号 41, p. 29247-29251, 発行日 2013-10-11
旧ID 48772
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