Evidence map›Paper›PMID 40106348›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Entropy is an important design principle in the photosystem II supercomplex.

Johanna L Hall, Shiun-Jr Yang, David T Limmer, Graham R Fleming

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Johanna L HallDepartment of Chemistry, University of California, Berkeley, CA 94720.ORCID 0000-0002-2784-2932
Shiun-Jr YangDepartment of Chemistry, University of California, Berkeley, CA 94720.ORCID 0009-0000-0524-8222
David T LimmerDepartment of Chemistry, University of California, Berkeley, CA 94720.ORCID 0000-0002-2766-0688
Graham R FlemingDepartment of Chemistry, University of California, Berkeley, CA 94720.ORCID 0000-0003-0847-1838

Funding

Alfred P. Sloan Foundation (APSF) NAKAVLI Energy Nanoscience Institute at Berkeley NAUS Department of Energy, Office of Science, Basic Energy Sciences, Chemical Sciences, Geosciences, and Biosciences Division FWP 449A 449BUS Department of Energy, Office of Science, Basic Energy Sciences, CPIMS Program Early Career Research Program DEFOA0002019
6 · The paper itself

Abstract

Photosystem II (PSII) can achieve near-unity quantum efficiency of light harvesting in ideal conditions and can dissipate excess light energy as heat to prevent the formation of reactive oxygen species (ROS) under light stress. Understanding how this pigment-protein complex accomplishes these opposing goals is a topic of great interest that has so far been explored primarily through the lens of the system energetics. Despite PSII's known flat energy landscape, a thorough consideration of the entropic effects on energy transfer in PSII is lacking. In this work, we aim to discern the free energetic design principles underlying the PSII energy transfer network. To accomplish this goal, we employ a structure-based rate matrix and compute the free energy terms in time following a specific initial excitation to discern how entropy and enthalpy drive ensemble system dynamics. We find that the interplay between the entropy and enthalpy components differ among each protein subunit, which allows each subunit to fulfill a unique role in the energy transfer network. This individuality ensures that PSII can accomplish efficient energy trapping in the reaction center (RC), effective nonphotochemical quenching (NPQ) in the periphery, and robust energy trapping in the other-monomer RC if the same-monomer RC is closed. We also show that entropy, in particular, is a dynamically tunable feature of the PSII free energy landscape accomplished through regulation of LHCII binding. These findings help rationalize natural photosynthesis and provide design principles for more efficient solar energy harvesting technologies.

Indexed as

EntropyPhotosystem II Protein ComplexEnergy TransferLight-Harvesting Protein ComplexesPhotosynthesisLight-Harvesting Protein ComplexesPhotosystem II Protein Complexenergy landscapeensemble dynamicsentropyexcitation energy transferfree energy

Identifiers

PMID40106348
PMCPMC11962461

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.