Ultrafast energy transfer between lipid-linked chromophores and plant light-harvesting complex II

Hancock, Ashley M.; Son, Minjung; Nairat, Muath; Wei, Tiejun; Jeuken, Lars J. C.; Duffy, Christopher D. P.; Schlau-Cohen, Gabriela S.; Adams, Peter G.

doi:10.1039/D1CP01628H

Title: Ultrafast energy transfer between lipid-linked chromophores and plant light-harvesting complex II

Journal Article · Wed Sep 15 00:00:00 EDT 2021 · Physical Chemistry Chemical Physics. PCCP

DOI:https://doi.org/10.1039/D1CP01628H· OSTI ID:1815202

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School of Physics and Astronomy, University of Leeds, Leeds LS2 9JT, UK, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA 02139, USA
School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, UK
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK, Leiden Institute of Chemistry, Leiden University, 2300 RA Leiden, The Netherlands

Light-Harvesting Complex II (LHCII) is a membrane protein found in plant chloroplasts that has the crucial role of absorbing solar energy and subsequently performing excitation energy transfer to the reaction centre subunits of Photosystem II. LHCII provides strong absorption of blue and red light, however, it has minimal absorption in the green spectral region where solar irradiance is maximal. In a recent proof-of-principle study, we enhanced the absorption in this spectral range by developing a biohybrid system where LHCII proteins together with lipid-linked Texas Red (TR) chromophores were assembled into lipid membrane vesicles. The utility of these systems was limited by significant LHCII quenching due to protein–protein interactions and heterogeneous lipid structures. Here, we organise TR and LHCII into a lipid nanodisc, which provides a homogeneous, well-controlled platform to study the interactions between TR molecules and single LHCII complexes. Fluorescence spectroscopy determined that TR-to-LHCII energy transfer has an efficiency of at least 60%, resulting in a 262% enhancement of LHCII fluorescence in the 525–625 nm range, two-fold greater than in the previous system. Ultrafast transient absorption spectroscopy revealed two time constants of 3.7 and 128 ps for TR-to-LHCII energy transfer. Structural modelling and theoretical calculations indicate that these timescales correspond to TR–lipids that are loosely- or tightly-associated with the protein, respectively, with estimated TR-to-LHCII separations of ~3.5 nm and ~1 nm. Overall, we demonstrate that a nanodisc-based biohybrid system provides an idealised platform to explore the photophysical interactions between extrinsic chromophores and membrane proteins with potential applications in understanding more complex natural or artificial photosynthetic systems.

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Research Organization:: Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)

Sponsoring Organization:: USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division

Grant/Contract Number:: SC0018097

OSTI ID:: 1815202

Alternate ID(s):: OSTI ID: 1852497

Journal Information:: Physical Chemistry Chemical Physics. PCCP, Journal Name: Physical Chemistry Chemical Physics. PCCP Vol. 23 Journal Issue: 35; ISSN 1463-9076

Publisher:: Royal Society of Chemistry (RSC)Copyright Statement

Country of Publication:: United Kingdom

Language:: English

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Journal Article · Mon Oct 01 00:00:00 EDT 2018 · Biochimica et Biophysica Acta - Bioenergetics · OSTI ID:1815202

Adams, Peter G.; Vasilev, Cvetelin; Hunter, C. Neil; +1 more

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
71 CLASSICAL AND QUANTUM MECHANICS
GENERAL PHYSICS

Title: Ultrafast energy transfer between lipid-linked chromophores and plant light-harvesting complex II

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