Assignment of red antenna states in photosystem I from Thermosynechococcus elongatus by single-molecule spectroscopy.
Single-molecule spectroscopy at cryogenic temperatures was used to elucidate spectral properties, heterogeneities, and dynamics of the chlorophyll a (Chla) molecules responsible for the fluorescence in photosystem I (PSI) from the cyanobacteria Thermosynechococcus elongatus. Absorption and hole burning data suggest the presence of three pools absorbing at wavelengths greater than 700 nm with their absorption maxima at 708, 715, and 719 nm. The responsible Chla molecules are termed C708, C715, and C719. In the emission spectra of single PSI complexes, zero-phonon lines (ZPLs) were observed over the whole red emission range of PSI. The spectral region of the C708 pool is dominated by intense ZPLs; on the other hand, the broad emission of C715/C719 is unstructured and ZPLs are seen in this region much less frequently. Spectral jumps of ZPLs were observed. The dynamics as well as the spectral range covered by such jumps differ for C708 and C715/C719. This heterogeneity is likely caused by differences in the close environment of the chromophores. A tentative assignment of C708 and C715/C719 to Chla dimers and a Chla trimer is discussed, which is based on the remarkable structural differences in the environment of the most probable candidates for the red-most fluorescence.
Brecht
Marc
M
Fachbereich Physik, Freie Universität Berlin, Arnimalle 14, 14195 Berlin, Germany.
Studier
Hauke
H
Elli
Alexandra F
AF
Jelezko
Fedor
F
Bittl
Robert
R
D002734:Chlorophyll / Q000737:chemistry*; D000077194:Chlorophyll A; D000458:Cyanobacteria / Q000737:chemistry*; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D045331:Photosystem I Protein Complex / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D045331:Photosystem I Protein Complex; D002734:Chlorophyll; D000077194:Chlorophyll A