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Photocurrent and electronic activities of oriented-His-tagged photosynthetic light-harvesting/reaction center core complexes assembled onto a gold electrode.
Kondo, Masaharu; Iida, Kouji; Dewa, Takehisa; Tanaka, Hirofumi; Ogawa, Takuji; Nagashima, Sakiko; Nagashima, Kenji V P; Shimada, Keizo; Hashimoto, Hideki; Gardiner, Alastair T; Cogdell, Richard J; Nango, Mamoru.
Afiliação
  • Kondo M; Department of Frontier Materials, Tsukuri College, Graduate School of Engineering, Nagoya Institute of Technology , Gokiso-cho, Showa-ku, Nagoya 466-8555, Japan.
Biomacromolecules ; 13(2): 432-8, 2012 Feb 13.
Article em En | MEDLINE | ID: mdl-22239547
ABSTRACT
A polyhistidine (His) tag was fused to the C- or N-terminus of the light-harvesting (LH1)-α chain of the photosynthetic antenna core complex (LH1-RC) from Rhodobacter sphaeroides to allow immobilization of the complex on a solid substrate with defined orientation. His-tagged LH1-RCs were adsorbed onto a gold electrode modified with Ni-NTA. The LH1-RC with the C-terminal His-tag (C-His LH1-RC) on the modified electrode produced a photovoltaic response upon illumination. Electron transfer is unidirectional within the RC and starts when the bacteriochlorophyll a dimer in the RC is activated by light absorbed by LH1. The LH1-RC with the N-terminal His-tag (N-His LH1-RC) produced very little or no photocurrent upon illumination at any wavelength. The conductivity of the His-tagged LH1-RC was measured with point-contact current imaging atomic force microscopy, indicating that 60% of the C-His LH1-RC are correctly oriented (N-His 63%). The oriented C-His LH1-RC or N-His LH1-RC showed semiconductive behavior, that is, had the opposite orientation. These results indicate that the His-tag successfully controlled the orientation of the RC on the solid substrate, and that the RC produced photocurrent depending upon the orientation on the electrode.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Rhodobacter sphaeroides / Materiais Biomiméticos / Complexos de Proteínas Captadores de Luz / Ouro Idioma: En Revista: Biomacromolecules Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Japão

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Rhodobacter sphaeroides / Materiais Biomiméticos / Complexos de Proteínas Captadores de Luz / Ouro Idioma: En Revista: Biomacromolecules Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Japão