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Carotenoid to chlorophyll energy transfer in the peridinin-chlorophyll-a-protein complex involves an intramolecular charge transfer state

Zigmantas, Donatas LU orcid ; Hiller, RG ; Sundström, Villy LU and Polivka, Tomas LU (2002) In Proceedings of the National Academy of Sciences 99(26). p.16760-16765
Abstract
Carotenoids are, along with chlorophylls, crucial pigments involved in light-harvesting processes in photosynthetic organisms. Details of carotenoid to chlorophyll energy transfer mechanisms and their dependence on structural variability of carotenoids are as yet poorly understood. Here, we employ femtosecond transient absorption spectroscopy to reveal energy transfer pathways in the peridinin-chlorophyll-a-protein (PCP) complex containing the highly substituted carotenoid peridinin, which includes an intramolecular charge transfer (ICT) state in its excited state manifold. Extending the transient absorption spectra toward near-infrared region (600-1800 nm) allowed us to separate contributions from different low-lying excited states of... (More)
Carotenoids are, along with chlorophylls, crucial pigments involved in light-harvesting processes in photosynthetic organisms. Details of carotenoid to chlorophyll energy transfer mechanisms and their dependence on structural variability of carotenoids are as yet poorly understood. Here, we employ femtosecond transient absorption spectroscopy to reveal energy transfer pathways in the peridinin-chlorophyll-a-protein (PCP) complex containing the highly substituted carotenoid peridinin, which includes an intramolecular charge transfer (ICT) state in its excited state manifold. Extending the transient absorption spectra toward near-infrared region (600-1800 nm) allowed us to separate contributions from different low-lying excited states of peridinin. The results demonstrate a special light-harvesting strategy in the PCP complex that uses the ICT state of peridinin to enhance energy transfer efficiency. (Less)
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publishing date
type
Contribution to journal
publication status
published
subject
in
Proceedings of the National Academy of Sciences
volume
99
issue
26
pages
16760 - 16765
publisher
National Academy of Sciences
external identifiers
  • wos:000180101600047
  • scopus:0037168673
ISSN
1091-6490
DOI
10.1073/pnas.262537599
language
English
LU publication?
yes
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The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Chemical Physics (S) (011001060)
id
ae0ea8f3-75b8-43f3-a355-e5bbc49bb516 (old id 320542)
date added to LUP
2016-04-01 12:16:09
date last changed
2022-01-27 01:17:28
@article{ae0ea8f3-75b8-43f3-a355-e5bbc49bb516,
  abstract     = {{Carotenoids are, along with chlorophylls, crucial pigments involved in light-harvesting processes in photosynthetic organisms. Details of carotenoid to chlorophyll energy transfer mechanisms and their dependence on structural variability of carotenoids are as yet poorly understood. Here, we employ femtosecond transient absorption spectroscopy to reveal energy transfer pathways in the peridinin-chlorophyll-a-protein (PCP) complex containing the highly substituted carotenoid peridinin, which includes an intramolecular charge transfer (ICT) state in its excited state manifold. Extending the transient absorption spectra toward near-infrared region (600-1800 nm) allowed us to separate contributions from different low-lying excited states of peridinin. The results demonstrate a special light-harvesting strategy in the PCP complex that uses the ICT state of peridinin to enhance energy transfer efficiency.}},
  author       = {{Zigmantas, Donatas and Hiller, RG and Sundström, Villy and Polivka, Tomas}},
  issn         = {{1091-6490}},
  language     = {{eng}},
  number       = {{26}},
  pages        = {{16760--16765}},
  publisher    = {{National Academy of Sciences}},
  series       = {{Proceedings of the National Academy of Sciences}},
  title        = {{Carotenoid to chlorophyll energy transfer in the peridinin-chlorophyll-a-protein complex involves an intramolecular charge transfer state}},
  url          = {{http://dx.doi.org/10.1073/pnas.262537599}},
  doi          = {{10.1073/pnas.262537599}},
  volume       = {{99}},
  year         = {{2002}},
}