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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of the electron carrier domain of the reaction center cytochrome c(z) subunit from green photosynthetic bacterium Chlorobium tepidum.
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Crystal structure of the electron carrier domain of the reaction center cytochrome c(z) subunit from green photosynthetic bacterium Chlorobium tepidum.

机译：绿色光合作用细菌淡绿绿藻的反应中心细胞色素c（z）亚基的电子载体结构域的晶体结构。

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In green sulfur photosynthetic bacteria, the cytochrome c(z) (cyt c(z)) subunit in the reaction center complex mediates electron transfer mainly from menaquinol/cytochrome c oxidoreductase to the special pair (P840) of the reaction center. The cyt c(z) subunit consists of an N-terminal transmembrane domain and a C-terminal soluble domain that binds a single heme group. The periplasmic soluble domain has been proposed to be highly mobile and to fluctuate between oxidoreductase and P840 during photosynthetic electron transfer. We have determined the crystal structure of the oxidized form of the C-terminal functional domain of the cyt c(z) subunit (C-cyt c(z)) from thermophilic green sulfur bacterium Chlorobium tepidum at 1.3-A resolution. The overall fold of C-cyt c(z) consists of four alpha-helices and is similar to that of class I cytochrome c proteins despite the low similarity in their amino acid sequences. The N-terminal structure of C-cyt c(z) supports the swinging mechanism previously proposed in relation with electron transfer, and the surface properties provide useful information on possible interaction sites with its electron transfer partners. Several characteristic features are observed for the heme environment: These include orientation of the axial ligands with respect to the heme plane, surface-exposed area of the heme, positions of water molecules, and hydrogen-bond network involving heme propionate groups. These structural features are essential for elucidating the mechanism for regulating the redox state of cyt c(z).
机译：在绿色硫磺光合细菌中，反应中心复合物中的细胞色素c（z）（cyt c（z））亚基主要介导电子从薄荷醇/细胞色素c氧化还原酶转移到反应中心的特殊对（P840）。 cyt c（z）亚基由结合单个血红素基团的N端跨膜结构域和C端可溶性结构域组成。已经提出周质可溶性结构域是高度可移动的并且在光合电子转移期间在氧化还原酶和P840之间波动。我们已经确定了从嗜热的绿色硫细菌淡绿梭菌（Clorobium tepidum）的cyt c（z）亚基（C-cyt c（z））C端功能域的C端功能域的氧化形式的晶体结构，分辨率为1.3-A。 C-cyt c（z）的整体折叠由四个α-螺旋组成，并且与I类细胞色素c蛋白相似，尽管它们的氨基酸序列相似性很低。 C-cyt c（z）的N末端结构支持先前提出的与电子转移有关的摆动机制，并且表面性质提供了有关与其电子转移伙伴可能相互作用的位置的有用信息。在血红素环境中观察到了几个特征：这些特征包括轴向配体相对于血红素平面的方向，血红素的表面暴露区域，水分子的位置以及涉及丙酸血红素酯基团的氢键网络。这些结构特征对于阐明调节cyt c（z）的氧化还原状态的机制至关重要。

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