4.7 Article

Structure of cyanobacterial photosystem I complexed with ferredoxin at 1.97 Å resolution

期刊

COMMUNICATIONS BIOLOGY
卷 5, 期 1, 页码 -

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NATURE PORTFOLIO
DOI: 10.1038/s42003-022-03926-4

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资金

  1. JST-CREST [JPMJCR20E1]
  2. MEXT-KAKENHI [21H02417]
  3. Platform Project for Supporting Drug Discovery and Life Science Research from AMED [JP20am0101117, JP16K07266, JP22ama121001j0001]
  4. Cyclic Innovation for Clinical Empowerment (CiCLE) grant from AMED [JP17pc0101020]
  5. National Research Foundation of Korea (NRF) - Korean government [2019R1A2C1004954]
  6. National Research Council of Science & Technology (NST) - Korean government [CCL22061-100]
  7. KBSI fund [C220000, C230130, C280320, C270100]
  8. Deutsche Forschungsgemeinschaft (DFG)
  9. China Scholarship Council (CSC) [201706220064]
  10. National Research Foundation of Korea [2019R1A2C1004954] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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By studying the high-resolution structure of the cyanobacterial photosystem I complexed with Ferredoxin, we have explained the details of its electron transfer process and proposed a possible mechanism for electron transfer. This helps us to better understand the function of Photosystem I.
In order to aid the understanding of the electron transfer process within the cyanobacterial photosystem I, its structure - when complexed with Ferredoxin - is determined at 1.97 angstrom resolution. Photosystem I (PSI) is a light driven electron pump transferring electrons from Cytochrome c(6) (Cyt c(6)) to Ferredoxin (Fd). An understanding of this electron transfer process is hampered by a paucity of structural detail concerning PSI:Fd interface and the possible binding sites of Cyt c(6). Here we describe the high resolution cryo-EM structure of Thermosynechococcus elongatus BP-1 PSI in complex with Fd and a loosely bound Cyt c(6). Side chain interactions at the PSI:Fd interface including bridging water molecules are visualized in detail. The structure explains the properties of mutants of PsaE and PsaC that affect kinetics of Fd binding and suggests a molecular switch for the dissociation of Fd upon reduction. Calorimetry-based thermodynamic analyses confirms a single binding site for Fd and demonstrates that PSI:Fd complexation is purely driven by entropy. A possible reaction cycle for the efficient transfer of electrons from Cyt c(6) to Fd via PSI is proposed.

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