Cited by 111Spectroscopy and Quantum Chemical StudiesPhotosynthetic Processes and MechanismsPhotochemistry and Electron Transfer Studies

Controlled Disorder in Plant Light-Harvesting Complex II Explains Its Photoprotective Role

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Krüger, Tjaart P.J., Ilioaia, Cristian, Johnson, Matthew P., Ruban, Alexander V., Papagiannakis, Emmanouil, Horton, Peter, van Grondelle, Rienk·2012·Biophysical Journal

Abstract

The light-harvesting antenna of photosystem II (PSII) has the ability to switch rapidly between a state of efficient light use and one in which excess excitation energy is harmlessly dissipated as heat, a process known as qE. We investigated the single-molecule fluorescence intermittency of the main component of the PSII antenna (LHCII) under conditions that mimic efficient use of light or qE, and we demonstrate that weakly fluorescing states are stabilized under qE conditions. Thus, we propose that qE is explained by biological control over the intrinsic dynamic disorder in the complex-the frequencies of switching establish whether the population of complexes is unquenched or quenched. Furthermore, the quenched states were accompanied by two distinct spectral signatures, suggesting more than one mechanism for energy dissipation in LHCII.

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Crossref · 10.1016/j.bpj.2012.04.044

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  • Static disorder also strongly affects the fate of an excitation in a light-harvesting complex by changing the probability of the excitation to be trapped in an energy sink or by pigment clusters that are not neighbouring other complexes in the photosystem.

    “Static disorder also strongly affects the fate of an excitation in a light-harvesting complex by changing the probability of the excitation to be trapped in an energy sink [63,64] or by pigment clusters that are not neighbouring other complexes in the photosystem [65].”

    From The future of quantum biology (2018) · cites this paper as [63]

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Authors
Krüger, T. P. J., Ilioaia, C., Johnson, M. P., Ruban, A. V., Papagiannakis, E., Horton, P., & van Grondelle, R.
Affiliations
  • Vrije Universiteit Amsterdam (NL)
  • Queen Mary University of London (GB)
  • University of Sheffield (GB)
Venue
Biophysical Journal
Publisher
Elsevier BV
Published
2012-06
Volume
102
Issue
11
Pages
2669-2676
ISSN
0006-3495 (ISSN-L)
OpenAlex
W2059440145
Cited by
111
References
39
Citations by year
2026: 4 · 2025: 4 · 2024: 5 · 2023: 1 · 2022: 6 · 2021: 6 · 2020: 5 · 2019: 7 · 2018: 9 · 2017: 14 · 2016: 11 · 2015: 13 · 2014: 14 · 2013: 9 · 2012: 3
FWCI
6.44
Type
journal article
Language
en
Open access
Locations
  • Biophysical Journal (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • VU Research Portal (submittedVersion, other-oa)
  • Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
Funders
  • Nederlandse Organisatie voor Wetenschappelijk Onderzoek (700.58.305, 267333)
  • Directorate for Biological Sciences
  • Engineering and Physical Sciences Research Council
  • Biotechnology and Biological Sciences Research Council
Topics
  • Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
Keywords
light-harvesting complex II, photosystem II, non-photochemical quenching, qE, dynamic disorder, energy dissipation, spectral signatures, photoprotection
MeSH terms
Centrifugation, Density Gradient, Fluorescence, Models, Molecular, Pigments, Biological, Spectrometry, Fluorescence, Thermodynamics, Protein Structure, Secondary, Spinacia oleracea, Photosystem II Protein Complex, Light-Harvesting Protein Complexes, Protein Multimerization, Photochemical Processes

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