Titlebar

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

 

Structural Variations in Chlorosomes from Wild-Type and a bchQR Mutant of Chlorobaculum tepidum Revealed by Single-Molecule Spectroscopy

Titelangaben

Günther, Lisa M. ; Löhner, Alexander ; Reiher, Carolin ; Kunsel, Tenzin ; Jansen, Thomas L. C. ; Tank, Marcus ; Bryant, Donald A. ; Knoester, Jasper ; Köhler, Jürgen:
Structural Variations in Chlorosomes from Wild-Type and a bchQR Mutant of Chlorobaculum tepidum Revealed by Single-Molecule Spectroscopy.
In: The Journal of Physical Chemistry B. Bd. 122 (4 Juni 2018) Heft 26 . - S. 6712-6723.
ISSN 1520-5207
DOI: https://doi.org/10.1021/acs.jpcb.8b02875

Abstract

Green sulfur bacteria can grow photosynthetically by absorbing only a few photons per bacteriochlorophyll molecule per day. They contain chlorosomes, perhaps the most efficient light-harvesting antenna system found in photosynthetic organisms. Chlorosomes contain supramolecular structures comprising hundreds of thousands of bacteriochlorophyll molecules, which are properly positioned with respect to one another solely by self-assembly and not by using a protein scaffold as a template for directing the mutual arrangement of the monomers. These two features-high efficiency and self-assembly-have attracted considerable attention for developing light-harvesting systems for artificial photosynthesis. However, reflecting the heterogeneity of the natural system, detailed structural information at atomic resolution of the molecular aggregates is not yet available. Here, we compare the results for chlorosomes from the wild type and two mutants of Chlorobaculum tepidum obtained by polarization-resolved, single-particle fluorescence-excitation spectroscopy and theoretical modeling with results previously obtained from nuclear-magnetic resonance spectroscopy and cryo-electron microscopy. Only the combination of information obtained from all of these techniques allows for an unambiguous description of the molecular packing of bacteriochlorophylls within chlorosomes. In contrast to some suggestions in the literature, we find that, for the chlorosomes from the wild type as well as for those from mutants, the dominant secondary structural element features tubular symmetry following a very similar construction principle. Moreover, the results suggest that the various options for methylation of the bacteriochlorophyll molecules, which are a primary source of the structural (and spectral) heterogeneity of wild-type chlorosome samples, are exploited by nature to achieve improved spectral coverage at the level of individual chlorosomes.

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: 19 Jul 2018 08:46
Letzte Änderung: 19 Jul 2018 08:46
URI: https://eref.uni-bayreuth.de/id/eprint/45128