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Inter-pigment interactions in the peridinin chlorophyll protein studied by global and target analysis of time resolved absorption spectra

van Stokkum, Ivo H. M.; Papagiannakis, Emmanouil; Vengris, Mikas; Salverda, Jante M.; Polivka, Tomas LU ; Zigmantas, Donatas LU ; Larsen, Delmar S.; Lampoura, Stefania S.; Hiller, Roger G. and van Grondelle, Rienk (2009) In Chemical Physics 357(1-3). p.70-78
Abstract
Inter-pigment interactions define the functioning of light-harvesting protein complexes. To describe the particularly complex molecular dynamics and interactions of peridinin and chlorophyll in the peridinin chlorophyll protein of Amphidinium carterae, we applied global and target analysis to a series of ultrafast transient absorption experiments. We have created and validated a model that consistently describes and characterizes the interactions and evolution of excited and ground-state populations after excitation in all different experiments. The series of energy transfer steps that follow excitation are described by our model of cascading populations and numerous rate constants that correspond to intra-molecular thermal relaxation,... (More)
Inter-pigment interactions define the functioning of light-harvesting protein complexes. To describe the particularly complex molecular dynamics and interactions of peridinin and chlorophyll in the peridinin chlorophyll protein of Amphidinium carterae, we applied global and target analysis to a series of ultrafast transient absorption experiments. We have created and validated a model that consistently describes and characterizes the interactions and evolution of excited and ground-state populations after excitation in all different experiments. The series of energy transfer steps that follow excitation are described by our model of cascading populations and numerous rate constants that correspond to intra-molecular thermal relaxation, fast and slow peridinin-to-chlorophyll energy transfer steps, and chlorophyll excited-state annihilation. By analyzing the spectral response of ground-state peridinins to excited chlorophylls we have identified which specific peridinin molecule is most closely coupled to the chlorophylls. No evidence was found that the intra-molecular charge transfer (ICT) state of peridinin, identified in studies of peridinin in solution, is a separate entity in the protein. The peridinin that exhibited slow peridinin-to-chlorophyll energy transfer was characterized by a difference spectrum free from ICT features, consistent with the importance of coupled ICT and S, states for energy transfer. (c) 2008 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
resolved absorption spectroscopy, Time, Global analysis, Peridinin chlorophyll protein, Target analysis
in
Chemical Physics
volume
357
issue
1-3
pages
70 - 78
publisher
Elsevier
external identifiers
  • wos:000263851800010
  • scopus:59649114302
ISSN
0301-0104
DOI
10.1016/j.chemphys.2008.10.005
language
English
LU publication?
yes
id
e2eebcb7-e3fc-4f94-9a05-937155863d3f (old id 1370727)
date added to LUP
2009-05-08 14:54:48
date last changed
2017-10-29 03:56:11
@article{e2eebcb7-e3fc-4f94-9a05-937155863d3f,
  abstract     = {Inter-pigment interactions define the functioning of light-harvesting protein complexes. To describe the particularly complex molecular dynamics and interactions of peridinin and chlorophyll in the peridinin chlorophyll protein of Amphidinium carterae, we applied global and target analysis to a series of ultrafast transient absorption experiments. We have created and validated a model that consistently describes and characterizes the interactions and evolution of excited and ground-state populations after excitation in all different experiments. The series of energy transfer steps that follow excitation are described by our model of cascading populations and numerous rate constants that correspond to intra-molecular thermal relaxation, fast and slow peridinin-to-chlorophyll energy transfer steps, and chlorophyll excited-state annihilation. By analyzing the spectral response of ground-state peridinins to excited chlorophylls we have identified which specific peridinin molecule is most closely coupled to the chlorophylls. No evidence was found that the intra-molecular charge transfer (ICT) state of peridinin, identified in studies of peridinin in solution, is a separate entity in the protein. The peridinin that exhibited slow peridinin-to-chlorophyll energy transfer was characterized by a difference spectrum free from ICT features, consistent with the importance of coupled ICT and S, states for energy transfer. (c) 2008 Elsevier B.V. All rights reserved.},
  author       = {van Stokkum, Ivo H. M. and Papagiannakis, Emmanouil and Vengris, Mikas and Salverda, Jante M. and Polivka, Tomas and Zigmantas, Donatas and Larsen, Delmar S. and Lampoura, Stefania S. and Hiller, Roger G. and van Grondelle, Rienk},
  issn         = {0301-0104},
  keyword      = {resolved absorption spectroscopy,Time,Global analysis,Peridinin chlorophyll protein,Target analysis},
  language     = {eng},
  number       = {1-3},
  pages        = {70--78},
  publisher    = {Elsevier},
  series       = {Chemical Physics},
  title        = {Inter-pigment interactions in the peridinin chlorophyll protein studied by global and target analysis of time resolved absorption spectra},
  url          = {http://dx.doi.org/10.1016/j.chemphys.2008.10.005},
  volume       = {357},
  year         = {2009},
}