Hancock, AM orcid.org/0000-0003-2069-5105, Son, M orcid.org/0000-0002-8385-062X, Nairat, M orcid.org/0000-0002-6384-584X et al. (5 more authors) (2021) Ultrafast energy transfer between lipid-linked chromophores and plant light-harvesting complex II. Physical Chemistry Chemical Physics, 23 (35). pp. 19511-19524. ISSN 1463-9076
Abstract
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © the Owner Societies 2021. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) > Molecular & Nanoscale Physics |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/T00004X/1 EPSRC (Engineering and Physical Sciences Research Council) EP/T013958/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 16 Sep 2021 13:10 |
Last Modified: | 09 Jan 2025 09:43 |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/d1cp01628h |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:178253 |