Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $$d$$ and $$f$$
Abstract
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 ChlD1 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 themore »
- Authors:
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[1];
[2];
[3];
[2];
[1];
[1];
[4];
[2];
[5];
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[7];
[1];
[2]
- Yale Univ., New Haven, CT (United States)
- Pennsylvania State Univ., University Park, PA (United States)
- Pennsylvania State Univ., University Park, PA (United States); National Taiwan University, Taipei (Taiwan)
- 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)
- Publication Date:
- Research Org.:
- Yale Univ., New Haven, CT (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; National Science Foundation (NSF)
- OSTI Identifier:
- 1860618
- Grant/Contract Number:
- FG02-05ER15646; SC0001423; SC0005291; MCB-1613022
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Biological Chemistry
- Additional Journal Information:
- Journal Volume: 298; Journal Issue: 1; Journal ID: ISSN 0021-9258
- Publisher:
- American Society for Biochemistry and Molecular Biology
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; photosystem II; far-red light photoacclimation; energy transfer; electron transfer; chlorophyll f; chlorophyll d; bicarbonate; photosynthesis; cyanobacteria; cryo-EM
Citation Formats
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., and Bryant, Donald A. Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $d$ and $f$. United States: N. p., 2021.
Web. doi:10.1016/j.jbc.2021.101424.
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. Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $d$ and $f$. United States. https://doi.org/10.1016/j.jbc.2021.101424
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., and Bryant, Donald A. Fri .
"Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $d$ and $f$". United States. https://doi.org/10.1016/j.jbc.2021.101424. https://www.osti.gov/servlets/purl/1860618.
@article{osti_1860618,
title = {Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $d$ and $f$},
author = {Gisriel, Christopher J. and Shen, Gaozhong and Ho, Ming-Yang and Kurashov, Vasily and Flesher, David A. and Wang, Jimin and Armstrong, William H. and Golbeck, John H. and Gunner, Marilyn R. and Vinyard, David J. and Debus, Richard J. and Brudvig, Gary W. and Bryant, Donald A.},
abstractNote = {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 ChlD1 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.},
doi = {10.1016/j.jbc.2021.101424},
journal = {Journal of Biological Chemistry},
number = 1,
volume = 298,
place = {United States},
year = {Fri Nov 19 00:00:00 EST 2021},
month = {Fri Nov 19 00:00:00 EST 2021}
}
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