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Structural insights into NDH-1 mediated cyclic electron transfer

Author

Listed:
  • Chunli Zhang

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Institute of Precision Medicine
    Phil River Technology)

  • Jin Shuai

    (Chinese Academy of Sciences (CAS)
    University of Chinese Academy of Sciences, CAS)

  • Zhaoxing Ran

    (Shanghai Normal University)

  • Jiaohong Zhao

    (Shanghai Normal University)

  • Zhenfang Wu

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Institute of Precision Medicine)

  • Rijing Liao

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Institute of Precision Medicine)

  • Jian Wu

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Institute of Precision Medicine
    Shanghai Key Laboratory of Translational Medicine on Ear and Nose diseases)

  • Weimin Ma

    (Shanghai Normal University
    Shanghai Normal University)

  • Ming Lei

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Institute of Precision Medicine
    Shanghai Jiao Tong University School of Medicine)

Abstract

NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus. The structure reveals three β-carotene and fifteen lipid molecules in the membrane arm of NDH-1L. Regulatory oxygenic photosynthesis-specific (OPS) subunits NdhV, NdhS and NdhO are close to the Fd-binding site whilst NdhL is adjacent to the plastoquinone (PQ) cavity, and they play different roles in PSI CET under high-light stress. NdhV assists in the binding of Fd to NDH-1L and accelerates PSI CET in response to short-term high-light exposure. In contrast, prolonged high-light irradiation switches on the expression and assembly of the NDH-1MS complex, which likely contains no NdhO to further accelerate PSI CET and reduce ROS production. We propose that this hierarchical mechanism is necessary for the survival of cyanobacteria in an aerobic environment.

Suggested Citation

  • Chunli Zhang & Jin Shuai & Zhaoxing Ran & Jiaohong Zhao & Zhenfang Wu & Rijing Liao & Jian Wu & Weimin Ma & Ming Lei, 2020. "Structural insights into NDH-1 mediated cyclic electron transfer," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14732-z
    DOI: 10.1038/s41467-020-14732-z
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    Cited by:

    1. Lvqin Zheng & Zhengdong Zhang & Hongrui Wang & Zhenggao Zheng & Jiayu Wang & Heyuan Liu & Hailong Chen & Chunxia Dong & Guopeng Wang & Yuxiang Weng & Ning Gao & Jindong Zhao, 2023. "Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Huili Sun & Guodong Luan & Yifan Ma & Wenjing Lou & Rongze Chen & Dandan Feng & Shanshan Zhang & Jiahui Sun & Xuefeng Lu, 2023. "Engineered hypermutation adapts cyanobacterial photosynthesis to combined high light and high temperature stress," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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