Resonance Raman characterization of Rhodobacter capsulatus reaction centers with lysine mutations near the accessory bacteriochlorophylls.
Resonance Raman characterization of Rhodobacter capsulatus reaction centers with lysine mutations near the accessory bacteriochlorophylls.
复制标题
荚膜红杆菌反应中心的共振拉曼表征，其赖氨酸突变靠近辅助细菌叶绿素。
DOI：
10.1007/s11120-004-2349-z
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发表时间：
2005
影响因子：
3.7
通讯作者：
Bocian,DavidF
中科院分区：
文献类型：
--
作者：
Chen,Lei;Kirmaier,Christine;Holten,Dewey;Bocian,DavidF
赖氨酸残基已被引入到红杆菌胶囊反应中心的M-多肽第201位和L-多肽第178位。这些位置分别位于辅助细菌叶绿体BA和BB的V环附近。共振拉曼研究表明，在M201或L178位引入Lys残基会导致BCHL辅因子的结构扰动。L178位的Lys与Bb直接作用，很可能是通过氢键。在S(L178)K/G(M201)D/L(M212)H三个突变体与G(M201)D/L(M212)H双突变体(C.Kirmaier等人)的RCS中观察到的氢键相互作用与增强的B分支电子转移是一致的。(1999年)生物化学38 11516-11530)相反，与在M201引入组氨酸相反，在M201引入Lys不会导致与BAcofactor的氢键(L.Chen等人)。(2004年)《物理化学》3108：0457-10464)。相应地，M201残基上赖氨酸侧链的烷基铵头基似乎与BA相距较远。
Lysine residues have been introduced intoRhodobacter capsulatusreaction centers at M-polypeptide position 201 and at L-polypeptide position 178. These positions are in the proximity of ring V of the accessory bacterochlorophylls BAand BB, respectively. Resonance Raman studies indicate that the introduction of a Lys residue at either position M201 or L178 results in structural perturbations to the BChl cofactors. Lys at L178 directly interacts with BB, most likely via a hydrogen bond. The hydrogen bonding interaction is consistent with enhanced B branch electron transfer that is observed in RCs from the S(L178)K/G(M201)D/L(M212)H triple mutant versus the G(M201)D/L(M212)H double mutant (C. Kirmaier et al. (1999) Biochemistry 38 11516–11530). In contrast, the introduction of a Lys at M201 does not result in hydrogen bonding to the BAcofactor, in contrast to the introduction of a His at M201 (L. Chen et al. (2004) J Phys Chem 3 108: 0457–10464). Accordingly, the alkyl ammonium head group of the side chain of the Lys at M201 residue appears to be distant from BA.