The photoprotective molecular switch in the photosystem II antenna
Open accessAbstract
We have reviewed the current state of multidisciplinary knowledge of the photoprotective mechanism in the photosystem II antenna underlying non-photochemical chlorophyll fluorescence quenching (NPQ). The physiological need for photoprotection of photosystem II and the concept of feed-back control of excess light energy are described. The outline of the major component of nonphotochemical quenching, qE, is suggested to comprise four key elements: trigger (ΔpH), site (antenna), mechanics (antenna dynamics) and quencher(s). The current understanding of the identity and role of these qE components is presented. Existing opinions on the involvement of protons, different LHCII antenna complexes, the PsbS protein and different xanthophylls are reviewed. The evidence for LHCII aggregation and macrostructural reorganization of photosystem II and their role in qE are also discussed. The models describing the qE locus in LHCII complexes, the pigments involved and the evidence for structural dynamics within single monomeric antenna complexes are reviewed. We suggest how PsbS and xanthophylls may exert control over qE by controlling the affinity of LHCII complexes for protons with reference to the concepts of hydrophobicity, allostery and hysteresis. Finally, the physics of the proposed chlorophyll-chlorophyll and chlorophyll-xanthophyll mechanisms of energy quenching is explained and discussed. This article is part of a Special Issue entitled: Photosystem II.
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NPQ functions to prevent photooxidative stress and is activated by feedbacks from the chloroplast reduction state and ATP demand.
“NPQ functions to prevent photooxidative stress (Li et al., 2009) and is activated by feedbacks from the chloroplast reduction state and ATP demand (Ruban et al., 2012).”
From Leaf Energy Balance Requires Mitochondrial Respiration and Export of Chloroplast NADPH in the Light (2019) · cites this paper as Ruban et al., 2012
Ruban et al. is cited for the activation clause, not the preceding photoprotection clause. Section 1.1 describes NPQ as a proton-mediated feedback process linked to ATP/NADPH production, and section 2 says its major high-light component is triggered by a proton gradient. The passages do not establish that feedback from the chloroplast reduction state and ATP demand specifically activates NPQ; they describe those relationships more indirectly. Page numbers are unavailable in our copy. (LLM, conf=0.82)
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Research works printed but not linked: 23
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- Authors
- Ruban, A. V., Johnson, M. P., & Duffy, C. D. P.
- Affiliations
- Queen Mary University of London (GB)
- Corresponding author
- Ruban, Alexander V.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2012-01
- Volume
- 1817
- Issue
- 1
- Pages
- 167-181
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2161324059
- Cited by
- 750
- References
- 0
- Citations by year
- 2026: 29 · 2025: 31 · 2024: 37 · 2023: 35 · 2022: 49 · 2021: 61 · 2020: 70 · 2019: 61 · 2018: 39 · 2017: 48 · 2016: 55 · 2015: 75 · 2014: 65 · 2013: 52 · 2012: 38
- FWCI
- 4.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- UK BBSRC
- EPSRC
- The Royal Society
- EU
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Keywords
- photoprotection, photosystem II, non-photochemical quenching, qE, light-harvesting complex II, PsbS protein, xanthophylls, allosteric regulation, hysteresis
- MeSH terms
- Chlorophyll, Fluorescence, Hydrogen-Ion Concentration, Protein Binding, Protons, Xanthophylls, Photosystem II Protein Complex, Zeaxanthins
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