Stability enhancement of cytochrome c through heme deprotonation and mutations
Biophysical Chemistry 139 巻 1 号
37-41 頁
2009-01 発行
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| ファイル情報(添付) | |
| タイトル ( eng ) |
Stability enhancement of cytochrome c through heme deprotonation and mutations
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| 作成者 |
Sonoyama Takafumi
Hasegawa Jun
Uchiyama Susumu
Nakamura Shota
Kobayashi Yuji
Sambongi Yoshihiro
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| 収録物名 |
Biophysical Chemistry
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| 巻 | 139 |
| 号 | 1 |
| 開始ページ | 37 |
| 終了ページ | 41 |
| 抄録 |
The chemical denaturation of Pseudomonas aeruginosa cytochrome c551 variants was examined at pH 5.0 and 3.6. All variants were stabilized at both pHs compared with the wild-type. Remarkably, the variants carrying the F34Y and/or E43Y mutations were more stabilized than those having the F7A/V13M or V78I ones at pH 5.0 compared with at pH 3.6 by ~3.0 – 4.6 kJ/mol. Structural analyses predicted that the side chains of introduced Tyr-34 and Tyr-43 become hydrogen donors for the hydrogen bond formation with heme 17-propionate at pH 5.0, but less efficiently at pH 3.6, because the propionate is deprotonated at the higher pH. Our results provide an insight into a stabilization strategy for heme proteins involving variation of the heme electronic state and introduction of appropriate mutations.
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| 著者キーワード |
Circular dichroism spectroscopy
Cytochrome c
Hydrogen bond
Protein stability
Heme propionate
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| NDC分類 |
生物科学・一般生物学 [ 460 ]
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| 言語 |
英語
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| 資源タイプ | 学術雑誌論文 |
| 出版者 |
Elsevier Science BV
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| 発行日 | 2009-01 |
| 権利情報 |
Copyright (c) 2008 Elsevier B.V.
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| 出版タイプ | Author’s Original（十分な品質であるとして、著者から正式な査読に提出される版） |
| アクセス権 | オープンアクセス |
| 収録物識別子 |
[ISSN] 0301-4622
[DOI] 10.1016/j.bpc.2008.09.020
[NCID] AA00566084
[DOI] http://dx.doi.org/10.1016/j.bpc.2008.09.020
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