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Four-wave-mixing spectroscopy of peridinin in solution and in the peridinin-chlorophyll-a protein

Christensson, Niklas LU ; Chabera, Pavel; Hiller, Roger G.; Pullerits, Tönu LU and Polivka, Tomas (2010) In Chemical Physics 373(1-2). p.15-22
Abstract
A model for the third order optical response of carotenoids is used to analyse transient grating and pump-probe data of peridinin in solution and bound in the peridinin-chlorophyll protein (PCP). For peridinin in solution, the transient grating signal detected at 505 nm exhibits a bi-exponential recovery whose fast phase is assigned to relaxation from the S-2 state that has a lifetime of 75 +/- 25 fs. The slower, solvent-dependent rise component is assigned to equilibration of the (S-1/ICT) state, taking place on a time scale of 0.6 and similar to 2.5 ps in acetontrile and benzene, respectively. These dynamics match those obtained from pump-probe measured in the spectral region of the ICT state, implying that the ICT state contributes to... (More)
A model for the third order optical response of carotenoids is used to analyse transient grating and pump-probe data of peridinin in solution and bound in the peridinin-chlorophyll protein (PCP). For peridinin in solution, the transient grating signal detected at 505 nm exhibits a bi-exponential recovery whose fast phase is assigned to relaxation from the S-2 state that has a lifetime of 75 +/- 25 fs. The slower, solvent-dependent rise component is assigned to equilibration of the (S-1/ICT) state, taking place on a time scale of 0.6 and similar to 2.5 ps in acetontrile and benzene, respectively. These dynamics match those obtained from pump-probe measured in the spectral region of the ICT state, implying that the ICT state contributes to the signal at 505 nm. In PCP, the transient grating signal shows distinctly different kinetics, and the signal shows no recovery. This difference is explained by energy transfer from peridinin to chlorophyll-a. (C) 2009 Elsevier B. V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Transient grating, Peridinin, Peridinin-chlorophyll protein
in
Chemical Physics
volume
373
issue
1-2
pages
15 - 22
publisher
Elsevier
external identifiers
  • wos:000280065100004
  • scopus:77955485065
ISSN
0301-0104
DOI
10.1016/j.chemphys.2009.12.011
language
English
LU publication?
yes
id
9a6a6591-82b9-49ce-9a7e-1bf8f3bbaf39 (old id 1656807)
date added to LUP
2010-08-31 12:38:29
date last changed
2018-06-17 04:03:19
@article{9a6a6591-82b9-49ce-9a7e-1bf8f3bbaf39,
  abstract     = {A model for the third order optical response of carotenoids is used to analyse transient grating and pump-probe data of peridinin in solution and bound in the peridinin-chlorophyll protein (PCP). For peridinin in solution, the transient grating signal detected at 505 nm exhibits a bi-exponential recovery whose fast phase is assigned to relaxation from the S-2 state that has a lifetime of 75 +/- 25 fs. The slower, solvent-dependent rise component is assigned to equilibration of the (S-1/ICT) state, taking place on a time scale of 0.6 and similar to 2.5 ps in acetontrile and benzene, respectively. These dynamics match those obtained from pump-probe measured in the spectral region of the ICT state, implying that the ICT state contributes to the signal at 505 nm. In PCP, the transient grating signal shows distinctly different kinetics, and the signal shows no recovery. This difference is explained by energy transfer from peridinin to chlorophyll-a. (C) 2009 Elsevier B. V. All rights reserved.},
  author       = {Christensson, Niklas and Chabera, Pavel and Hiller, Roger G. and Pullerits, Tönu and Polivka, Tomas},
  issn         = {0301-0104},
  keyword      = {Transient grating,Peridinin,Peridinin-chlorophyll protein},
  language     = {eng},
  number       = {1-2},
  pages        = {15--22},
  publisher    = {Elsevier},
  series       = {Chemical Physics},
  title        = {Four-wave-mixing spectroscopy of peridinin in solution and in the peridinin-chlorophyll-a protein},
  url          = {http://dx.doi.org/10.1016/j.chemphys.2009.12.011},
  volume       = {373},
  year         = {2010},
}