中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

文献类型:期刊论文

作者Kawakami, Tomoaki; Yu, Long-Jiang; Liang, Tai; Okazaki, Koudai; Madigan, Michael T.; Kimura, Yukihiro2; Wang-Otomo, Zheng-Yu
刊名NATURE COMMUNICATIONS
出版日期2021
卷号12期号:1
DOI10.1038/s41467-021-21397-9
文献子类Article
英文摘要Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems. The high potential iron-sulfur (HiPIP) proteins are direct electron donors to the light-harvesting-reaction center complexes (LH1-RC) in photosynthetic beta- and gamma -Proteobacteria. Here, the authors present the 2.9 angstrom crystal structure of the HiPIP-bound LH1-RC complex from the thermophilic purple sulfur bacterium Thermochromatium tepidum and discuss mechanistic implications for the electron transfer pathway.
学科主题Multidisciplinary Sciences
出版地BERLIN
电子版国际标准刊号2041-1723
WOS关键词TETRAHEME CYTOCHROME SUBUNIT ; IRON-SULFUR PROTEIN ; INTERACTION SITE ; BACTERIUM ; BINDING ; C(2) ; THERMOSTABILITY ; THERMODYNAMICS ; COMPENSATION ; FERREDOXIN
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
语种英语
WOS记录号WOS:000621232800023
出版者NATURE PORTFOLIO
资助机构JSPS KAKENHI [JP16H04174, JP18H05153, JP20H05086, JP20H02856] ; Takeda Science Foundation ; Kurata Memorial Hitachi Science and Technology Foundation, Japan ; grant of KINOU-KYOKA from Institute of Quantum Beam Science of Ibaraki University ; National Key R&D Program of China [2019YFA0904600]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/26704]  
专题中科院光生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Photosynth Res Ctr, Beijing, Peoples R China
2.Madigan, Michael T.] Southern Illinois Univ, Dept Microbiol, Carbondale, IL USA
3.Kobe Univ, Grad Sch Agr, Dept Agrobiosci, Kobe, Hyogo, Japan
4.Ibaraki Univ, Fac Sci, Mito, Ibaraki, Japan
推荐引用方式
GB/T 7714
Kawakami, Tomoaki,Yu, Long-Jiang,Liang, Tai,et al. Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP[J]. NATURE COMMUNICATIONS,2021,12(1).
APA Kawakami, Tomoaki.,Yu, Long-Jiang.,Liang, Tai.,Okazaki, Koudai.,Madigan, Michael T..,...&Wang-Otomo, Zheng-Yu.(2021).Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP.NATURE COMMUNICATIONS,12(1).
MLA Kawakami, Tomoaki,et al."Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP".NATURE COMMUNICATIONS 12.1(2021).

入库方式: OAI收割

来源:植物研究所

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