著作: [植野 哲]/[柴田 瑩]/Ayako Yorimitsu/[馬場 嘉信]/Kamo Naoki/Redox potentials of the oriented film of the wild-type, the E194Q-, E204Q- and D96N-mutated bacteriorhodopsin/[Biochimica et Biophysica Acta (BBA) - Biomembranes]
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種別 | 必須 | 学術論文(審査論文) | |||
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言語 | 必須 | 英語 | |||
招待 | 推奨 | ||||
審査 | 推奨 | Peer Review | |||
カテゴリ | 推奨 | ||||
共著種別 | 推奨 | ||||
学究種別 | 推奨 | ||||
組織 | 推奨 |
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著者 | 必須 | ||||
題名 | 必須 |
(英) Redox potentials of the oriented film of the wild-type, the E194Q-, E204Q- and D96N-mutated bacteriorhodopsin |
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副題 | 任意 | ||||
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. |
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キーワード | 推奨 |
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発行所 | 推奨 | Elsevier Science B.V. | |||
誌名 | 必須 |
Biochimica et Biophysica Acta (BBA) - Biomembranes([Elsevier Science])
(pISSN: 0005-2736, eISSN: 1879-2642)
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巻 | 必須 | 1609 | |||
号 | 必須 | 1 | |||
頁 | 必須 | 109 114 | |||
都市 | 任意 | ||||
年月日 | 必須 | 2003年 1月 10日 | |||
URL | 任意 | ||||
DOI | 任意 | 10.1016/S0005-2736(02)00660-0 (→Scopusで検索) | |||
PMID | 任意 | 12507765 (→Scopusで検索) | |||
CRID | 任意 | ||||
WOS | 任意 | ||||
Scopus | 任意 | ||||
評価値 | 任意 | ||||
被引用数 | 任意 | ||||
指導教員 | 推奨 | ||||
備考 | 任意 |
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