Putative hydrogen bond to tyrosine M208 in photosynthetic reaction centers from Rhodobacter capsulatus significantly slows primary charge separation.

Putative hydrogen bond to tyrosine M208 in photosynthetic reaction centers from Rhodobacter capsulatus significantly slows primary charge separation.
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DOI:
10.1021/jp503422c
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发表时间:
2014-06-19
期刊:
The journal of physical chemistry. B
影响因子:
--
通讯作者:
Kirmaier C
Kirmaier C
中科院分区:
其他
文献类型:
--
作者:
Saggu M;Carter B;Zhou X;Faries K;Cegelski L;Holten D;Boxer SG;Kirmaier C

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在 M208 处带有天然 Tyr 残基以及 M204 处异亮氨酸向谷氨酸的单个氨基酸变化的荚膜红杆菌反应中心 (RC) 中观察到缓慢的约 50 ps、P* → P+HA– 电子转移。在室温下,P* 衰变动力学异常均匀(单指数)。 [4'-13C]Tyr 标记的野生型和 M204E RC 的比较固态 NMR 显示,Tyr M208 的化学位移在 M204E 突变体中显着改变,并且改变的方式与与 Tyr M208 羟基形成氢键一致。基于 RC 晶体结构坐标的模型表明,如果在 M204 处的 Glu 和 M208 Tyr 羟基之间形成这样的氢键,则 -OH 将以预期的方式取向(基于 Alden 等人,J. Phys. Chem.1996, 100, 16761–16770 的计算),从而使自由能中的 P+BA– 不稳定。 Glu M204 通过这种假定的氢键改变 Tyr M208 和 BA 的环境,对初级电荷分离具有强大的影响。
Slow, ∼50 ps, P* → P+HA– electron transfer is observed in Rhodobacter capsulatus reaction centers (RCs) bearing the native Tyr residue at M208 and the single amino acid change of isoleucine at M204 to glutamic acid. The P* decay kinetics are unusually homogeneous (single exponential) at room temperature. Comparative solid-state NMR of [4′-13C]Tyr labeled wild-type and M204E RCs show that the chemical shift of Tyr M208 is significantly altered in the M204E mutant and in a manner consistent with formation of a hydrogen bond to the Tyr M208 hydroxyl group. Models based on RC crystal structure coordinates indicate that if such a hydrogen bond is formed between the Glu at M204 and the M208 Tyr hydroxyl group, the −OH would be oriented in a fashion expected (based on the calculations by Alden et al., J. Phys. Chem.1996, 100, 16761–16770) to destabilize P+BA– in free energy. Alteration of the environment of Tyr M208 and BA by Glu M204 via this putative hydrogen bond has a powerful influence on primary charge separation.
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