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DOI | 10.1038/nature24672 |
Structure of the complex I-like molecule NDH of oxygenic photosynthesis | |
Laughlin, Thomas G.1,2; Bayne, Andrew N.3,4; Trempe, Jean-Francois3,4; Savage, David F.1; Davies, Karen M.1,2 | |
2019-02-21 | |
发表期刊 | NATURE |
ISSN | 0028-0836 |
EISSN | 1476-4687 |
出版年 | 2019 |
卷号 | 566期号:7744页码:411-+ |
文章类型 | Article |
语种 | 英语 |
国家 | USA; Canada |
英文摘要 | Cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis(1,2). NAD(P)H dehydrogenase-like complex (NDH) is a key component of this pathway in most oxygenic photosynthetic organisms(3,4) and is the last large photosynthetic membrane-protein complex for which the structure remains unknown. Related to the respiratory NADH dehydrogenase complex (complex I), NDH transfers electrons originating from PSI to the plastoquinone pool while pumping protons across the thylakoid membrane, thereby increasing the amount of ATP produced per NADP+ molecule reduced(4,5). NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants(3,6). However, the three core complex I subunits that are involved in accepting electrons from NAD(P) H are notably absent in NDH3,5,6, and it is therefore not clear how NDH acquires and transfers electrons to plastoquinone. It is proposed that the OPS subunits-specifically NdhS-enable NDH to accept electrons from its electron donor, ferredoxin(3-5,7). Here we report a 3.1 angstrom structure of the 0.42-MDa NDH complex from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1, obtained by single-particle cryo-electron microscopy. Our maps reveal the structure and arrangement of the principal OPS subunits in the NDH complex, as well as an unexpected cofactor close to the plastoquinone-binding site in the peripheral arm. The location of the OPS subunits supports a role in electron transfer and defines two potential ferredoxin-binding sites at the apex of the peripheral arm. These results suggest that NDH could possess several electron transfer routes, which would serve to maximize plastoquinone reduction and avoid deleterious off-target chemistry of the semi-plastoquinone radical. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000459119200053 |
WOS关键词 | DEHYDROGENASE-LIKE COMPLEX ; FERREDOXIN-BINDING-SITE ; BEAM-INDUCED MOTION ; DOMAIN-LIKE FOLD ; CRYO-EM ; THERMOSYNECHOCOCCUS-ELONGATUS ; CRYSTAL-STRUCTURE ; ELECTRON-TRANSFER ; PROTEIN ; SUBUNIT |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/202827 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Calif Berkeley, Dept Mol & Cell Biol, 229 Stanley Hall, Berkeley, CA 94720 USA; 2.Lawrence Berkeley Natl Lab, Mol Biophys & Integrat Bioimaging Div, Berkeley, CA 94720 USA; 3.Grp Etud Proteines Membranaires GEPROM, Montreal, PQ, Canada; 4.McGill Univ, Dept Pharmacol & Therapeut, Montreal, PQ, Canada |
推荐引用方式 GB/T 7714 | Laughlin, Thomas G.,Bayne, Andrew N.,Trempe, Jean-Francois,et al. Structure of the complex I-like molecule NDH of oxygenic photosynthesis[J]. NATURE,2019,566(7744):411-+. |
APA | Laughlin, Thomas G.,Bayne, Andrew N.,Trempe, Jean-Francois,Savage, David F.,&Davies, Karen M..(2019).Structure of the complex I-like molecule NDH of oxygenic photosynthesis.NATURE,566(7744),411-+. |
MLA | Laughlin, Thomas G.,et al."Structure of the complex I-like molecule NDH of oxygenic photosynthesis".NATURE 566.7744(2019):411-+. |
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