Photoaffinity labeling of the phylloquinone‐binding polypeptides by 2‐azidoanthraquinone in photosystem I particles

FEBS Letters

Itoh, Shigeru¹  Iwaki, Masayo¹  Takahashi, Yuichiro³  Shimada, Keizo²  Takahashi, Masaaki⁴ 

[1] Division of Bioenergetics, National Institute for Basic Biology, Myodaiji, Okazaki 444, Japan;Department of Biology, Faculty of Science, Tokyo Metropolitan University, Minami-Osawa, Hachioji, Tokyo 192-03, Japan;Graduate School of Natural Science and Technology, and Department of Biology, Faculty of Science, Okayama University, Tsushima-naka, Okayama 700, Japan;Department of Biology, Faculty of Science, Konan University, Okamoto, Higashinada, Kobe 658, Japan

关键词: Photosystem I;    Reaction center;    Photoaffinity label;    Phylloquinone (vitamin K1);    Electron transfer;    AzAQ;    2-azido-9;    10-anthraquinone;    CBB;    Coomassie brilliant blue;    LDAO;    lauryldimethylamine oxide;    P700;    the primary donor chlorophyll a;    PS;    photosystem;    Qφ;    the secondary acceptor quinone;    RC;    reaction center;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(92)81403-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A photoaffinity label, 2-azido-9,10-anthraquinone, binds at the quinone-binding (Q_φ) site with high affinity and can substitute for the secondary acceptor, phylloquinone, in photosystem I reaction center of spinach. Phylloquinone-depleted photosystem I particles reconstituted with azido-[³H]anthraquinone were illuminated with UV light and analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis. The large core polypeptides (psaA and/or psaB) were selectively labeled. The labeling was competitively inhibited in the presence of anthraquinone. These results indicate that the Q_φ site is located on psaA or psaB polypeptides.

【 授权许可】

Unknown