Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase
复制标题
复合物I样光合NAD(P)H脱氢酶电子传递机制的结构基础
DOI：
10.1038/s41467-020-14456-0
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发表时间：
2020-01-30
影响因子：
16.6
通讯作者：
Li, Mei
中科院分区：
文献类型：
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作者：
Pan, Xiaowei;Cao, Duanfang;Li, Mei
蓝藻的NAD(P)H脱氢酶类(NDH)复合体NDH-1L在光系统I周围的循环电子流(CEF)和呼吸过程中起着至关重要的作用。NDH-1L偶联从铁氧还蛋白(FD)到质醌(PQ)的电子传递，并将质子从细胞质泵入管腔，从而驱动ATP的产生。依赖于NDH-1L的CEF增加了ATP/NADPH的比值，因此是有氧光养细胞在胁迫下发挥作用的关键。在这里，我们报道了来自长链热球菌BP-1的两个NDH-1L结构，分别与一个FD和一个内源PQ形成复合体。我们的结构代表了蓝藻NDH-1L的完整模型，揭示了NDH-1L与FD和PQ的结合方式，以及对NDH-1L复合体的正常功能至关重要的结构元件。总之，我们的数据为深入了解电子从FD到PQ的传输，以及它与NDH-1L中质子传输的耦合提供了深刻的见解。
NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress. Here we report two structures of NDH-1L from Thermosynechococcus elongatus BP-1, in complex with one Fd and an endogenous PQ, respectively. Our structures represent the complete model of cyanobacterial NDH-1L, revealing the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. Together, our data provides deep insights into the electron transport from Fd to PQ, and its coupling with proton translocation in NDH-1L.