Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $d$ and $f$

Gisriel, Christopher J.; Shen, Gaozhong; Ho, Ming-Yang; Kurashov, Vasily; Flesher, David A.; Wang, Jimin; Armstrong, William H.; Golbeck, John H.; Gunner, Marilyn R.; Vinyard, David J.; Debus, Richard J.; Brudvig, Gary W.; Bryant, Donald A.

doi:10.1016/j.jbc.2021.101424

Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $$d$$ and $$f$$

Journal Article · Fri Nov 19 00:00:00 EST 2021 · Journal of Biological Chemistry

DOI:https://doi.org/10.1016/j.jbc.2021.101424· OSTI ID:1860618

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Yale Univ., New Haven, CT (United States); Yale University
Pennsylvania State Univ., University Park, PA (United States)
Pennsylvania State Univ., University Park, PA (United States); National Taiwan University, Taipei (Taiwan)
Yale Univ., New Haven, CT (United States)
Boston College, Chestnut Hill, MA (United States)
City College of New York, NY (United States)
Louisiana State Univ., Baton Rouge, LA (United States)
Univ. of California, Riverside, CA (United States)

Far-red light (FRL) photoacclimation (FaRLiP) in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include far-red/near-infrared light (700 to 800 nm). During this photoacclimation process, photosystem II (PSII), the water:plastoquinone photooxidoreductase involved in oxygenic photosynthesis, is modified. The resulting FRL-PSII is comprised of FRL-specific core subunits and binds chlorophyll (Chl) d and Chl f molecules in place of several of the Chl a molecules found when cells are grown in visible light. These new Chls effectively lower the energy canonically thought to define the “red limit” for light required to drive photochemical catalysis of water oxidation. Changes to the architecture of FRL-PSII were previously unknown, and the positions of Chl d and Chl f molecules had only been proposed from indirect evidence. Here, we describe the 2.25-Å resolution cryo-EM structure of a monomeric FRL-PSII core complex from Synechococcus sp. PCC 7335 cells that were acclimated to FRL. We identify one Chl d molecule in the Chl_D1 position of the electron transfer chain, and four Chl f molecules in the core antenna. We also make observations that enhance our understanding of PSII biogenesis, especially on the acceptor side of the complex where a bicarbonate molecule is replaced by a glutamate sidechain in the absence of the assembly factor Psb28. In conclusion, these results provide a structural basis for the lower energy limit required to drive water oxidation, which is the gateway for most solar energy utilization on Earth.

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Research Organization:: Yale Univ., New Haven, CT (United States)

Sponsoring Organization:: National Science Foundation; USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division

Grant/Contract Number:: FG02-05ER15646; SC0001423; SC0005291

OSTI ID:: 1860618

Journal Information:: Journal of Biological Chemistry, Journal Name: Journal of Biological Chemistry Journal Issue: 1 Vol. 298; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light

Journal Article · Mon Dec 19 19:00:00 EST 2022 · Journal of Biological Chemistry · OSTI ID:2339806

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
bicarbonate
chlorophyll d
chlorophyll f
cryo-EM
cyanobacteria
electron transfer
energy transfer
far-red light photoacclimation
photosynthesis
photosystem II

Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $$d$$ and $$f$$

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