Your browser doesn't support javascript.
loading
Anomalous pH Effect of Blue Proteorhodopsin.
Yamada, Keisuke; Kawanabe, Akira; Yoshizawa, Susumu; Inoue, Kentaro; Kogure, Kazuhiro; Kandori, Hideki.
Afiliação
  • Yamada K; †Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
  • Kawanabe A; †Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
  • Yoshizawa S; ‡Atmosphere and Ocean Research Institute, The University of Tokyo, Kashiwa-shi, Chiba 277-8564, Japan.
  • Inoue K; ‡Atmosphere and Ocean Research Institute, The University of Tokyo, Kashiwa-shi, Chiba 277-8564, Japan.
  • Kogure K; ‡Atmosphere and Ocean Research Institute, The University of Tokyo, Kashiwa-shi, Chiba 277-8564, Japan.
  • Kandori H; †Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
J Phys Chem Lett ; 3(7): 800-4, 2012 Apr 05.
Article em En | MEDLINE | ID: mdl-26286400
ABSTRACT
Proteorhodopsin (PR) is a light-driven proton pump found in marine bacteria, and thousands of PRs are classified into blue-absorbing PR (B-PR; λmax ≈ 490 nm) and green-absorbing PR (G-PR; λmax ≈ 525 nm). In this report, we present conversion of B-PR into G-PR using anomalous pH effect. B-PR in LC1-200, marine γ-proteobacteria, absorbs 497 and 513 nm maximally at pH 7 and 4, respectively, whose pH titration was reversible (pKa = 4.8). When pH was lowered from 4, the λmax was further red-shifted (528 nm at pH 2). This is unusual because blue shift occurs by chloride binding in the case of bacteriorhodopsin. Surprisingly, when pH was increased from 2 to 7, the λmax of this B-PR was further red-shifted to 540 nm, indicating that green-absorbing PR (PR540) is created only by changing pH. The present study reports the conformational flexibility of microbial rhodopsins, leading to the switch of absorbing color by a simple pH change.
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: J Phys Chem Lett Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Japão

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: J Phys Chem Lett Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Japão