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Exciton Delocalization Promotes Far-Red Absorption in a Tetrameric Chlorophyll a Light-Harvesting Complex from Trachydiscus minutus

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F25%3A00646030" target="_blank" >RIV/60077344:_____/25:00646030 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/25:00646030 RIV/60076658:12310/25:43910790

  • Result on the web

    <a href="https://pubs.acs.org/doi/pdf/10.1021/jacs.5c17299?ref=article_openPDF" target="_blank" >https://pubs.acs.org/doi/pdf/10.1021/jacs.5c17299?ref=article_openPDF</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/jacs.5c17299" target="_blank" >10.1021/jacs.5c17299</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Exciton Delocalization Promotes Far-Red Absorption in a Tetrameric Chlorophyll a Light-Harvesting Complex from Trachydiscus minutus

  • Original language description

    Photosynthetic organisms employ light-harvesting complexes (LHCs) to optimize energy capture under variable light conditions. The freshwater eustigmatophyte Trachydiscus minutus accumulates a red-shifted violaxanthin-chlorophyll protein (rVCP) that contributes to far-red light harvesting using only chlorophyll (Chl) a molecules, without chemical modification or substitution of pigments. Based on high-resolution cryo-EM and multiscale quantum chemical calculations, we uncovered a heterodimer-based tetrameric architecture, representing a unique oligomerization mode among LHCs. Within each heterodimer, Chls a are distinctively arranged adjacent to the terminal emitter, forming an unprecedentedly extended chlorophyll cluster. Quantum chemical calculations reveal three strong exciton-coupled pigment domains, two of which reside in the large cluster and solely account for the intense far-red absorption near 700 nm without contributions from charge-transfer states. Our structural and quantum chemical characterizations of far-red light harvesting reveal a molecular mechanism of red spectral tuning that relies on protein-controlled excitonic coupling of identical Chl a pigments, as demonstrated here in this eustigmatophyte, highlighting diverse adaptations for harvesting spectrally shifted, low-energy light.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/EH22_008%2F0004624" target="_blank" >EH22_008/0004624: PHOTOMACHINES - Photosynthetic cell redesign for high yields of therapeutic peptides</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of the American Chemical Society

  • ISSN

    0002-7863

  • e-ISSN

    1520-5126

  • Volume of the periodical

    147

  • Issue of the periodical within the volume

    51

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

    47675-47689

  • UT code for WoS article

    001638309000001

  • EID of the result in the Scopus database

    2-s2.0-105025677468