Substitution of isoleucine L177 by histidine in Rhodobacter sphaeroides reaction center results in the covalent binding of PA bacteriochlorophyll to the L subunit
Substitution of isoleucine L177 by histidine in Rhodobacter sphaeroides reaction center results in the covalent binding of PA bacteriochlorophyll to the L subunit
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DOI：
10.1016/j.febslet.2007.11.032
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发表时间：
2007-12-22
期刊：
影响因子：
3.5
通讯作者：
Shuvalov, Vladimir A.
中科院分区：
文献类型：
--
作者：
Fufina, Tatiana Y.;Vasilieva, Lyudmila G.;Shuvalov, Vladimir A.
在这项工作中，我们报告了细菌叶绿素（BChl）的独特案例——由单一突变引起的光合膜复合物中的蛋白质共价附着。球形红细菌光合反应中心（RC）中的异亮氨酸 L177 被组氨酸取代。色素分析表明，I(L177) H RC 的丙酮-甲醇提取物中缺少一个 BChl 分子。 SDS-PAGE证明该BChl分子不能用有机溶剂提取，显然是因为它与突变体RC L-亚基稳定共价连接。我们的数据表明，附着的细菌叶绿素是特殊的 BChls、P-A 对之一。这种共价相互作用的化学性质仍有待确定。 (C) 2007 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
In this work, we report the unique case of bacteriochlorophyll (BChl) - protein covalent attachment in a photosynthetic membrane complex caused by a single mutation. The isoleucine L177 was substituted by histidine in the photosynthetic reaction center (RC) of Rhodobacter sphaeroides. Pigment analysis revealed that one BChl molecule was missing in the acetone - methanol extract of the I(L177) H RCs. SDS-PAGE demonstrated that this BChl molecule could not be extracted with organic solvents apparently because of its stable covalent attachment to the mutant RC L-subunit. Our data indicate that the attached bacteriochlorophyll is one of the special pair BChls, P-A. The chemical nature of this covalent interaction remains to be identified. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.