Probing the binding sites of exchanged chlorophyll a in LH2 by Raman and site‐selection fluorescence spectroscopies

FEBS Letters

Fraser, Niall J.³  Gall, Andrew¹  Bellissent-Funel, Marie-Claire¹  Robert, Bruno²  Cogdell, Richard J.³ 

[1] Laboratoire Léon Brillouin (CEA-CNRS), CEA-Saclay, 91191 Gif-sur-Yvette Cedex, France;Section de Biophysique des Protéines et des Membranes, DBCM/CEA and URA2096/CNRS, C.E. Saclay, 91191 Gif-sur-Yvette Cedex, France;Division of Biochemistry and Molecular Biology, IBLS, University of Glasgow, Glasgow G12 8QQ, UK

关键词: Bacteriochlorophyll;    Chlorophyll;    Fluorescence line-narrowing spectroscopy;    Raman spectroscopy;    Photosynthesis;    (B)Chla;    (bacterio)chlorophyll a (esterified with phytol);    (B)ChlX;    (bacterio)chlorophyll absorbing at X nm;    B800;    B850;    binding sites for Bchla absorbing at 800 and 850 nm;    respectively;    FLN;    fluorescence line narrowing;    LH;    light-harvesting;    Rps.;    Rhodopseudomonas;    Rb.;    Rhodobacter;    RR;    resonance Raman;    THF;    tetrahydrofuran;   

DOI  :  10.1016/S0014-5793(01)02161-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In this work we have selectively released the 800 nm absorbing bacteriochlorophyll a molecules of the LH2 protein from the photosynthetic bacterium Rhodopseudomonas acidophila, strain 10050, and replaced them with chlorophyll a (Chla). A combination of low-temperature electronic absorption, resonance Raman and site-selection fluorescence spectroscopies revealed that the Chla pigments are indeed bound in the B800 binding site; this is the first work that formally proves that such non-native chlorins can be inserted correctly into LH2.

【 授权许可】

Unknown