Bacteriochlorin-protein interactions in native B800-B850, B800 deficient and B800-Bchlap-reconstituted complexes from Rhodopseudomonas acidophila, strain 10050

被引:28
作者
Gall, A
Fraser, NJ
Bellissent-Funel, MC
Scheer, H
Robert, B [1 ]
Cogdell, RJ
机构
[1] CEA, DBCM, Serv Biophys Prot & Membranes, F-91191 Gif Sur Yvette, France
[2] CEA Saclay, CNRS, URA2096, F-91191 Gif Sur Yvette, France
[3] CEA Saclay, CNRS, Lab Leon Brillouin, F-91191 Gif Sur Yvette, France
[4] Univ Glasgow, Div Biochem & Mol Biol, Glasgow G12 8QQ, Lanark, Scotland
[5] Univ Munich, Inst Bot, D-80638 Munich, Germany
基金
英国生物技术与生命科学研究理事会;
关键词
bacteriochlorophyll; light harvesting complex; photosynthesis; pigment extraction;
D O I
10.1016/S0014-5793(99)00410-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:269 / 272
页数:4
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