| ○種別 (必須): | □ | 学術論文 (審査論文)
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| ○言語 (必須): | □ | 英語
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| ○招待 (推奨): |
| ○審査 (推奨): | □ | Peer Review
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| ○学究種別 (推奨): |
| ○組織 (推奨): | 1. | 徳島大学.大学院ヘルスバイオサイエンス研究部.生体情報薬科学部門.分子情報薬学講座 (2004年4月1日〜)
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| ○著者 (必須): | 1. | 植野 哲 ([徳島大学.大学院医歯薬学研究部.薬学域.薬科学部門.総合薬学教育学系.総合薬学研究推進学])
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| 2. | 柴田 瑩
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| 3. | (英) Ayako Yorimitsu (日) (読)
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| 4. | 馬場 嘉信
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| 5. | (英) Kamo Naoki (日) (読)
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| ○題名 (必須): | □ | (英) Redox potentials of the oriented film of the wild-type, the E194Q-, E204Q- and D96N-mutated bacteriorhodopsin (日)
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| ○要約 (任意): | □ | (英) The redox potentials of the oriented films of the wild-type, the E194Q-, E204Q- and D96N-mutated bacteriorhodopsins (bR), prepared by adsorbing purple membrane (PM) sheets or its mutant on a Pt electrode, have been examined. The redox potentials (V) of the wild-type bR were -470 mV for the 13-cis configuration of the retinal Shiff base in bR and -757 mV for the all-trans configuration in H(2)O, and -433 mV for the 13-cis configuration and -742 mV for the all-trans configuration in D(2)O. The solvent isotope effect (DeltaV=V(D(2)O)-V(H(2)O)), which shifts the redox potential to a higher value, originates from the cooperative rearrangements of the extensively hydrogen-bonded water molecules around the protonated C=N part in the retinal Schiff base. The redox potential of bR was much higher for the 13-cis configuration than that for the all-trans configuration. The redox potentials for the E194Q mutant in the extracellular region were -507 mV for the 13-cis configuration and -788 mV for the all-trans configuration; and for the E204Q mutant they were -491 mV for the 13-cis configuration and -769 mV for the all-trans configuration. Replacement of the Glu(194) or Glu(204) residues by Gln weakened the electron withdrawing interaction to the protonated C=N bond in the retinal Schiff base. The E204 residue is less linked with the hydrogen-bonded network of the proton release pathway compared with E194. The redox potentials of the D96N mutant in the cytoplasmic region were -471 mV for the 13-cis configuration and -760 mV for the all-trans configuration which were virtually the same as those of the wild-type bR, indicating that the D to N point mutation of the 96 residue had no influence on the interaction between the D96 residue and the C=N part in the Schiff base under the light-adapted condition. The results suggest that the redox potential of bR is closely correlated to the hydrogen-bonded network spanning from the retinal Schiff base to the extracellular surface of bR in the proton transfer pathway. (日)
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| ○キーワード (推奨): | 1. | (英) Redox potential (日) (読)
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| 2. | (英) Bacteriorhodopsin (日) (読)
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| 3. | (英) Mutant (日) (読)
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| 4. | (英) Shiff base (日) (読)
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| 5. | (英) Hydrogen-bonded network (日) (読)
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| ○発行所 (推奨): | □ | Elsevier Science B.V.
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| ○誌名 (必須): | □ | Biochimica et Biophysica Acta (BBA) - Biomembranes ([Elsevier Science])
(pISSN: 0005-2736, eISSN: 1879-2642)
| ○ISSN (任意): | □ | 0005-2736
ISSN: 0005-2736
(pISSN: 0005-2736, eISSN: 1879-2642) Title: Biochimica et biophysica acta. BiomembranesTitle(ISO): Biochim Biophys Acta BiomembrPublisher: Elsevier BV (NLM Catalog)
(Scopus)
(CrossRef)
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| ○巻 (必須): | □ | 1609
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| ○号 (必須): | □ | 1
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| ○頁 (必須): | □ | 109 114
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| ○都市 (任意): |
| ○年月日 (必須): | □ | 西暦 2003年 1月 10日 (平成 15年 1月 10日)
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| ○URL (任意): |
| ○DOI (任意): | □ | 10.1016/S0005-2736(02)00660-0 (→Scopusで検索)
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| ○PMID (任意): | □ | 12507765 (→Scopusで検索)
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| ○備考 (任意): | 1. | (英) Article.Affiliation: Faculty of Pharmaceutical Sciences, Tokushima University, Tokushima, Japan. (日)
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| 2. | (英) Article.PublicationTypeList.PublicationType: Journal Article (日)
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| 3. | (英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't (日)
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