Bacteriochlorin‐protein interactions in native B800‐B850, B800 deficient and B800‐Bchla p‐reconstituted complexes from Rhodopseudomonas acidophila, strain 10050

FEBS Letters

Fraser, Niall J.⁴  Gall, Andrew³  Bellissent-Funel, Marie-Claire¹  Scheer, Hugo²  Robert, Bruno³  Cogdell, Richard J.⁴ 

[1] Laboratoire Léon Brillouin (CEA-CNRS), CEA-Saclay, 91191 Gif-sur-Yvette Cedex, France;Botanisches Institut der Universität München, Menzinger Str. 67, D-80638 München, Germany;Section de Biophysique des Protéines et des Membranes, DBCM/CEA and URA2096/CNRS, CEA-Saclay, 91191 Gif-sur-Yvette Cedex, France;Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow G12 8QQ, UK

关键词: Bacteriochlorophyll;    Light harvesting complex;    Photosynthesis;    Pigment extraction;    Bchla;    bacteriochlorophyll a;    the esterifying alcohol is indicated by the subscript (p=phytol);    cm−1;    wavenumber;    H-bond;    hydrogen bond;    LH;    light harvesting;    RR;    resonance Raman;    B800;    B500;    binding sites for bacteriochlorophyll a p absorbing at 800 and 850 nm;    respectively;   

DOI  :  10.1016/S0014-5793(99)00410-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recently, a method which allows the selective release and removal of the 800 nm absorbing bacteriochlorophyll a (B800) molecules from the LH2 complex of Rhodopseudomonas acidophila strain 10050 has been described [Fraser, N.J. (1999) Ph.D. Thesis, University of Glasgow, UK]. This procedure also allows the reconstitution of empty binding sites with the native pigment Bchla _p, esterified with phytol. We have investigated the bacteriochlorophylla-protein interactions in native, B800 deficient (or B850) and in B800-bacteriochlorophylla _p-reconstituted LH2 complexes by resonance Raman spectroscopy. We present the first direct structural evidence which shows that the reconstituted pigments are correctly bound within their binding pockets.

【 授权许可】

Unknown