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Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls

Polivka, Tomas LU ; Pascher, Torbjörn LU ; Sundström, Villy LU and Hiller, RG (2005) In Photosynthesis Research 86(1-2). p.217-227
Abstract
In vitro studies of the carotenoid peridinin, which is the primary pigment from the peridinin chlorophyll-a protein (PCP) light harvesting complex, showed a strong dependence on the lifetime of the peridinin lowest singlet excited state on solvent polarity. This dependence was attributed to the presence of an intramolecular charge transfer (ICT) state in the peridinin excited state manifold. The ICT state was also suggested to be a crucial factor in efficient peridinin to Chl-a energy transfer in the PCP complex. Here we extend our studies of peridinin dynamics to reconstituted PCP complexes, in which Chl-a was replaced by different chlorophyll species (Chl-b, acetyl Chl-a, Chl-d and BChl-a). Reconstitution of PCP with different Chl... (More)
In vitro studies of the carotenoid peridinin, which is the primary pigment from the peridinin chlorophyll-a protein (PCP) light harvesting complex, showed a strong dependence on the lifetime of the peridinin lowest singlet excited state on solvent polarity. This dependence was attributed to the presence of an intramolecular charge transfer (ICT) state in the peridinin excited state manifold. The ICT state was also suggested to be a crucial factor in efficient peridinin to Chl-a energy transfer in the PCP complex. Here we extend our studies of peridinin dynamics to reconstituted PCP complexes, in which Chl-a was replaced by different chlorophyll species (Chl-b, acetyl Chl-a, Chl-d and BChl-a). Reconstitution of PCP with different Chl species maintains the energy transfer pathways within the complex, but the efficiency depends on the chlorophyll species. In the native PCP complex, the peridinin S-1/ICT state has a lifetime of 2.7 ps, whereas in reconstituted PCP complexes it is 5.9 ps (Chl-b) 2.9 ps (Chl-a), 2.2 ps (acetyl Chl-a), 1.9 ps (Chl-d), and 0.45 ps (BChl-a). Calculation of energy transfer rates using the Forster equation explains the differences in energy transfer efficiency in terms of changing spectral overlap between the peridinin emission and the absorption spectrum of the acceptor. It is proposed that the lowest excited state of peridinin is a strongly coupled S-1/ICT state, which is the energy donor for the major energy transfer channel. The significant ICT character of the S-1/ICT state in PCP enhances the transition dipole moment of the S-1/ICT state, facilitating energy transfer to chlorophyll via the Forster mechanism. In addition to energy transfer via the S-1/ICT, there is also energy transfer via the S-2 and hot S-1/ICT states to chlorophyll in all reconstituted PCP complexes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Photosynthesis Research
volume
86
issue
1-2
pages
217 - 227
publisher
Springer
external identifiers
  • wos:000231998200020
  • pmid:16172940
  • scopus:25444446803
ISSN
0166-8595
DOI
10.1007/s11120-005-1447-x
language
English
LU publication?
yes
id
fe63c4ea-881c-4070-96d0-2e13a61d3122 (old id 151829)
date added to LUP
2007-07-03 14:52:18
date last changed
2017-05-07 04:21:57
@article{fe63c4ea-881c-4070-96d0-2e13a61d3122,
  abstract     = {In vitro studies of the carotenoid peridinin, which is the primary pigment from the peridinin chlorophyll-a protein (PCP) light harvesting complex, showed a strong dependence on the lifetime of the peridinin lowest singlet excited state on solvent polarity. This dependence was attributed to the presence of an intramolecular charge transfer (ICT) state in the peridinin excited state manifold. The ICT state was also suggested to be a crucial factor in efficient peridinin to Chl-a energy transfer in the PCP complex. Here we extend our studies of peridinin dynamics to reconstituted PCP complexes, in which Chl-a was replaced by different chlorophyll species (Chl-b, acetyl Chl-a, Chl-d and BChl-a). Reconstitution of PCP with different Chl species maintains the energy transfer pathways within the complex, but the efficiency depends on the chlorophyll species. In the native PCP complex, the peridinin S-1/ICT state has a lifetime of 2.7 ps, whereas in reconstituted PCP complexes it is 5.9 ps (Chl-b) 2.9 ps (Chl-a), 2.2 ps (acetyl Chl-a), 1.9 ps (Chl-d), and 0.45 ps (BChl-a). Calculation of energy transfer rates using the Forster equation explains the differences in energy transfer efficiency in terms of changing spectral overlap between the peridinin emission and the absorption spectrum of the acceptor. It is proposed that the lowest excited state of peridinin is a strongly coupled S-1/ICT state, which is the energy donor for the major energy transfer channel. The significant ICT character of the S-1/ICT state in PCP enhances the transition dipole moment of the S-1/ICT state, facilitating energy transfer to chlorophyll via the Forster mechanism. In addition to energy transfer via the S-1/ICT, there is also energy transfer via the S-2 and hot S-1/ICT states to chlorophyll in all reconstituted PCP complexes.},
  author       = {Polivka, Tomas and Pascher, Torbjörn and Sundström, Villy and Hiller, RG},
  issn         = {0166-8595},
  language     = {eng},
  number       = {1-2},
  pages        = {217--227},
  publisher    = {Springer},
  series       = {Photosynthesis Research},
  title        = {Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls},
  url          = {http://dx.doi.org/10.1007/s11120-005-1447-x},
  volume       = {86},
  year         = {2005},
}