Bacteriochlorin-protein interactions in native B800-B850, B800 deficient and B800-Bchlap-reconstituted complexes from Rhodopseudomonas acidophila, strain 10050
Bacteriochlorin-protein interactions in native B800-B850, B800 deficient and B800-Bchlap-reconstituted complexes from Rhodopseudomonas acidophila, strain 10050
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DOI：
10.1016/s0014-5793(99)00410-x
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发表时间：
1999-04-23
期刊：
影响因子：
3.5
通讯作者：
Cogdell, RJ
中科院分区：
文献类型：
--
作者：
Gall, A;Fraser, NJ;Cogdell, RJ
最近，已经描述了一种允许从嗜酸红假单胞菌菌株 10050 的 LH2 复合物中选择性释放和去除 800 nm 吸收细菌叶绿素 a (B800) 分子的方法 [Fraser, N.J. (1999) 博士，论文，英国格拉斯哥大学]，该程序还允许用天然色素 Bchla(p) 重建空结合位点，我们通过共振拉曼光谱研究了天然、B800 缺陷（或 B850）和 B800-细菌叶绿素（p）-重建 LH2 复合物中细菌叶绿素-蛋白质相互作用。我们提出了第一个直接的结构证据，表明重构的颜料正确地结合在其结合袋内。 (C) 1999 年欧洲生化学会联合会。
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.