Titlebar

Bibliografische Daten exportieren
Literatur vom gleichen Autor
plus auf ERef Bayreuth
plus bei Google Scholar

 

Unified analysis of ensemble and single-complex optical spectral data from light-harvesting complex-2 chromoproteins for gaining deeper insight into bacterial photosynthesis

Titelangaben

Pajusalu, Mihkel ; Kunz, Ralf ; Rätsep, Margus ; Timpmann, Kõu ; Köhler, Jürgen ; Freiberg, Arvi:
Unified analysis of ensemble and single-complex optical spectral data from light-harvesting complex-2 chromoproteins for gaining deeper insight into bacterial photosynthesis.
In: Physical Review E. Bd. 92 (2015) Heft 5 . - Art.Nr. 052709.
ISSN 1550-2376
DOI: https://doi.org/10.1103/PhysRevE.92.052709

Abstract

Bacterial light-harvesting pigment-protein complexes are very efficient at converting photons into excitons and transferring them to reaction centers, where the energy is stored in a chemical form. Optical properties of the complexes are known to change significantly in time and also vary from one complex to another; therefore, a detailed understanding of the variations on the level of single complexes and how they accumulate into effects that can be seen on the macroscopic scale is required. While experimental and theoretical methods exist to study the spectral properties of light-harvesting complexes on both individual complex and bulk ensemble levels, they have been developed largely independently of each other. To fill this gap,, we simultaneously analyze experimental low-temperature single-complex and bulk ensemble optical spectra of the light-harvesting complelx- 2 (LH2) chromoproteins from the photosynthetic bacterium in order to find a unique theoretical model consistent with both experimental situations. The model, which satisfies most of the observations, combines strong exciton-phonon coupling with significant disorder, characteristic of the proteins. We establish a detailed disorder model that, in addition to containing a C2-symmetrical modulation of the site energies, distinguishes between static intercomplex and slow conformational intracomplex disorders. The model evaluations also verify that, despite best efforts, the single-LH2-complex measurements performed so fa may be biased toward complexes with higher Huang-Rhys- factors.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten > Fakultät für Mathematik, Physik und Informatik > Physikalisches Institut > Lehrstuhl Experimentalphysik IX - Spektroskopie weicher Materie > Lehrstuhl Experimentalphysik IX - Spektroskopie weicher Materie - Univ.-Prof. Dr. Jürgen Köhler
Fakultäten
Fakultäten > Fakultät für Mathematik, Physik und Informatik
Fakultäten > Fakultät für Mathematik, Physik und Informatik > Physikalisches Institut
Fakultäten > Fakultät für Mathematik, Physik und Informatik > Physikalisches Institut > Lehrstuhl Experimentalphysik IX - Spektroskopie weicher Materie
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 530 Physik
Eingestellt am: 12 Apr 2018 11:41
Letzte Änderung: 12 Apr 2018 11:41
URI: https://eref.uni-bayreuth.de/id/eprint/43378