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- Title
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase.
- Authors
Pan, Xiaowei; Cao, Duanfang; Xie, Fen; Xu, Fang; Su, Xiaodong; Mi, Hualing; Zhang, Xinzheng; Li, Mei
- Abstract
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. NAD(P)H dehydrogenase-like complex NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen. Here authors report two structures of NDH-1L from Thermosynechococcus elongatus BP-1, in complex with one Fd and an endogenous PQ, respectively.
- Subjects
ELECTRON transport; NAD (Coenzyme); PHOTOSYSTEMS; CYANOBACTERIAL toxins; PROTONS; NICOTINAMIDE adenine dinucleotide phosphate; CYTOPLASM
- Publication
Nature Communications, 2020, Vol 11, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-020-14456-0