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Light harvesting in purple bacteria does not rely on resonance fine-tuning in peripheral antenna complexes

Keil, Erika ; Lokstein, Heiko ; Cogdell, Richard ; Hauer, Jürgen ; Zigmantas, Donatas LU orcid and Thyrhaug, Erling LU (2024) In Photosynthesis Research 161(3). p.191-201
Abstract

The ring-like peripheral light-harvesting complex 2 (LH2) expressed by many phototrophic purple bacteria is a popular model system in biological light-harvesting research due to its robustness, small size, and known crystal structure. Furthermore, the availability of structural variants with distinct electronic structures and optical properties has made this group of light harvesters an attractive testing ground for studies of structure–function relationships in biological systems. LH2 is one of several pigment-protein complexes for which a link between functionality and effects such as excitonic coherence and vibronic coupling has been proposed. While a direct connection has not yet been demonstrated, many such interactions are highly... (More)

The ring-like peripheral light-harvesting complex 2 (LH2) expressed by many phototrophic purple bacteria is a popular model system in biological light-harvesting research due to its robustness, small size, and known crystal structure. Furthermore, the availability of structural variants with distinct electronic structures and optical properties has made this group of light harvesters an attractive testing ground for studies of structure–function relationships in biological systems. LH2 is one of several pigment-protein complexes for which a link between functionality and effects such as excitonic coherence and vibronic coupling has been proposed. While a direct connection has not yet been demonstrated, many such interactions are highly sensitive to resonance conditions, and a dependence of intra-complex dynamics on detailed electronic structure might be expected. To gauge the sensitivity of energy-level structure and relaxation dynamics to naturally occurring structural changes, we compare the photo-induced dynamics in two structurally distinct LH2 variants. Using polarization-controlled 2D electronic spectroscopy at cryogenic temperatures, we directly access information on dynamic and static disorder in the complexes. The simultaneous optimal spectral and temporal resolution of these experiments further allows us to characterize the ultrafast energy relaxation, including exciton transport within the complexes. Despite the variations in PPC molecular structure manifesting as clear differences in electronic structure and disorder, the energy-transport and—relaxation dynamics remain remarkably similar. This indicates that the light-harvesting functionality of purple bacteria within a single LH2 complex is highly robust to structural perturbations and likely does not rely on finely tuned electronic- or electron-vibrational resonance conditions.

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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Energy transfer, Excitons, Light-harvesting, Ultrafast spectroscopy
in
Photosynthesis Research
volume
161
issue
3
pages
11 pages
publisher
Springer
external identifiers
  • scopus:85196542305
  • pmid:38907135
ISSN
0166-8595
DOI
10.1007/s11120-024-01107-4
language
English
LU publication?
yes
id
0c2f7baa-156c-4f1e-b9ba-9a2060a45564
date added to LUP
2024-08-30 13:27:46
date last changed
2024-09-04 12:42:54
@article{0c2f7baa-156c-4f1e-b9ba-9a2060a45564,
  abstract     = {{<p>The ring-like peripheral light-harvesting complex 2 (LH2) expressed by many phototrophic purple bacteria is a popular model system in biological light-harvesting research due to its robustness, small size, and known crystal structure. Furthermore, the availability of structural variants with distinct electronic structures and optical properties has made this group of light harvesters an attractive testing ground for studies of structure–function relationships in biological systems. LH2 is one of several pigment-protein complexes for which a link between functionality and effects such as excitonic coherence and vibronic coupling has been proposed. While a direct connection has not yet been demonstrated, many such interactions are highly sensitive to resonance conditions, and a dependence of intra-complex dynamics on detailed electronic structure might be expected. To gauge the sensitivity of energy-level structure and relaxation dynamics to naturally occurring structural changes, we compare the photo-induced dynamics in two structurally distinct LH2 variants. Using polarization-controlled 2D electronic spectroscopy at cryogenic temperatures, we directly access information on dynamic and static disorder in the complexes. The simultaneous optimal spectral and temporal resolution of these experiments further allows us to characterize the ultrafast energy relaxation, including exciton transport within the complexes. Despite the variations in PPC molecular structure manifesting as clear differences in electronic structure and disorder, the energy-transport and—relaxation dynamics remain remarkably similar. This indicates that the light-harvesting functionality of purple bacteria within a single LH2 complex is highly robust to structural perturbations and likely does not rely on finely tuned electronic- or electron-vibrational resonance conditions.</p>}},
  author       = {{Keil, Erika and Lokstein, Heiko and Cogdell, Richard and Hauer, Jürgen and Zigmantas, Donatas and Thyrhaug, Erling}},
  issn         = {{0166-8595}},
  keywords     = {{Energy transfer; Excitons; Light-harvesting; Ultrafast spectroscopy}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{191--201}},
  publisher    = {{Springer}},
  series       = {{Photosynthesis Research}},
  title        = {{Light harvesting in purple bacteria does not rely on resonance fine-tuning in peripheral antenna complexes}},
  url          = {{http://dx.doi.org/10.1007/s11120-024-01107-4}},
  doi          = {{10.1007/s11120-024-01107-4}},
  volume       = {{161}},
  year         = {{2024}},
}