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  Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer.

Schuller, J. M., Birrell, J. A., Tanaka, H., Konuma, T., Wulfhorst, H., Cox, N., et al. (2019). Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science, 363(6424), 257-260. doi:10.1126/science.aau3613.

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© 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works http://www.sciencemag.org/about/science-licenses-journal-article-reuse

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 Creators:
Schuller, Jan M.1, Author           
Birrell, James A2, Author
Tanaka, Hideaki2, Author
Konuma, Tsuyoshi2, Author
Wulfhorst, Hannes2, Author
Cox, Nicholas2, Author
Schuller, Sandra K2, Author
Thiemann, Jacqueline2, Author
Lubitz, Wolfgang2, Author
Setif, Pierre2, Author
Ikegami, Takahisa2, Author
Engel, Benjamin D.3, Author           
Kurisu, Genji2, Author
Nowaczyk, Marc M2, Author
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              
3Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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 Abstract: Photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion. We report a 3.3-A resolution cryo-EM structure of photosynthetic complex I from the cyanobacterium Thermosynechococcus elongatus. The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. By mimicking cyclic electron flow with isolated components in vitro, we demonstrate that ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH. A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process. Copyright © 2018, American Association for the Advancement of Science.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 30573545
DOI: 10.1126/science.aau3613
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Title: Science
  Other : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 363 (6424) Sequence Number: - Start / End Page: 257 - 260 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1