Refinement of a structural model of a pigment-protein complex by accurate optical line shape theory and experiments

T. Renger, I. Trostmann, C. Theiss, Mohamed Madjet, M. Richter, H. Paulsen, H. J. Eichler, A. Knorr, G. Renger

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

Time-local and time-nonlocal theories are used in combination with optical spectroscopy to characterize the water-soluble chlorophyll binding protein complex (WSCP) from cauliflower. The recombinant cauliflower WSCP complexes reconstituted with either chlorophyll b (Chl b) or Chl a/Chl b mixtures are characterized by absorption spectroscopy at 77 and 298 K and circular dichroism at 298 K. On the basis of the analysis of these spectra and spectra reported for recombinant WSCP reconstituted with Chl a only (Hughes, J. L.; Razeghifard, R.; Logue, M.; Oakley, A.; Wydrzynski, T.; Krausz, E. J. Am. Chem. Soc. U.S.A. 2006, 128, 3649), the "open-sandwich" model proposed for the structure of the pigment dimer is refined. Our calculations show that, for a reasonable description of the data, a reduction of the angle between pigment planes from 60° of the original model to about 30° is required when exciton relaxation-induced lifetime broadening is included in the analysis of optical spectra. The temperature dependence of the absorption spectrum is found to provide a unique test for the two non-Markovian theories of optical spectra. Based on our data and the 1.7 K spectra of Hughes et al. (2006), the time-local partial ordering prescription theory is shown to describe the experimental results over the whole temperature range between 1.7 K and room temperature, whereas the alternative timenonlocal chronological ordering prescription theory fails at high temperatures. Modified-Redfield theory predicts sub-100 fs exciton relaxation times for the homodimers and a 450 fs time constant in the heterodimers. Whereas the simpler Redfield theory gives a similar time constant for the homodimers, the one for the heterodimers deviates strongly in the two theories. The difference is explained by multivibrational quanta transitions in the protein which are neglected in Redfield theory.

Original languageEnglish
Pages (from-to)10487-10501
Number of pages15
JournalJournal of Physical Chemistry B
Volume111
Issue number35
DOIs
Publication statusPublished - 6 Sep 2007
Externally publishedYes

Fingerprint

Chlorophyll Binding Proteins
chlorophylls
Chlorophyll
pigments
Pigments
line shape
proteins
Proteins
Water
Excitons
Experiments
time constant
optical spectrum
Temperature
excitons
water
Absorption spectroscopy
Dimers
Relaxation time
Dichroism

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Refinement of a structural model of a pigment-protein complex by accurate optical line shape theory and experiments. / Renger, T.; Trostmann, I.; Theiss, C.; Madjet, Mohamed; Richter, M.; Paulsen, H.; Eichler, H. J.; Knorr, A.; Renger, G.

In: Journal of Physical Chemistry B, Vol. 111, No. 35, 06.09.2007, p. 10487-10501.

Research output: Contribution to journalArticle

Renger, T, Trostmann, I, Theiss, C, Madjet, M, Richter, M, Paulsen, H, Eichler, HJ, Knorr, A & Renger, G 2007, 'Refinement of a structural model of a pigment-protein complex by accurate optical line shape theory and experiments', Journal of Physical Chemistry B, vol. 111, no. 35, pp. 10487-10501. https://doi.org/10.1021/jp0717241
Renger, T. ; Trostmann, I. ; Theiss, C. ; Madjet, Mohamed ; Richter, M. ; Paulsen, H. ; Eichler, H. J. ; Knorr, A. ; Renger, G. / Refinement of a structural model of a pigment-protein complex by accurate optical line shape theory and experiments. In: Journal of Physical Chemistry B. 2007 ; Vol. 111, No. 35. pp. 10487-10501.
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AU - Renger, T.

AU - Trostmann, I.

AU - Theiss, C.

AU - Madjet, Mohamed

AU - Richter, M.

AU - Paulsen, H.

AU - Eichler, H. J.

AU - Knorr, A.

AU - Renger, G.

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