4.6 Article

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

期刊

PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 23, 期 35, 页码 19511-19524

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cp01628h

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资金

  1. Engineering and Physical Sciences Research Council (EPSRC, UK) [1807029]
  2. EPSRC [EP/T013958/1, EP/J017566/1]
  3. U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, Division of Chemical Sciences, Geosciences, and Biosciences [DE-SC0018097]
  4. University Academic Fellowship from the University of Leeds
  5. Biotechnology and Biological Sciences Research Council (BBSRC) [BB/T00004X/1]
  6. Alan Turing Institute
  7. Chinese Scholarship Council
  8. BBSRC [BB/T000023/1]
  9. BBSRC [BB/T00004X/1, BB/T000023/1] Funding Source: UKRI
  10. EPSRC [1807029, EP/T013958/1] Funding Source: UKRI
  11. Engineering and Physical Sciences Research Council [EP/J017566/1] Funding Source: researchfish

向作者/读者索取更多资源

Light-Harvesting Complex II (LHCII) is a membrane protein that plays a crucial role in absorbing solar energy and transferring it to Photosystem II. A recent study enhanced absorption in the green spectral region by organizing TR and LHCII into a lipid nanodisc. Fluorescence spectroscopy showed a 60% efficiency in energy transfer and a 262% enhancement of LHCII fluorescence in the 525-625 nm range, with ultrafast transient absorption spectroscopy revealing two time constants for energy transfer. Structural modeling and theoretical calculations indicated different separations for TR-to-LHCII interactions, showcasing the potential of the nanodisc-based biohybrid system in exploring photophysical interactions between chromophores and membrane proteins.
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 similar to 3.5 nm and similar to 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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