Akademik Veri Yönetim Sistemi
BIOPHYSICAL JOURNAL, cilt.75, sa.6, ss.3064-3077, 1998 (SCI-Expanded)
Spectral and kinetic information on energy transfer within the light-harvesting complex II (LHCII) monomer was obtained from this subpicosecond transient absorption study, by using selective excitation (663, 669, 672, 678, and 682 nm) of various Chl a absorption bands and detecting the induced changes over the entire Q(y) region (650 -700 nm). It is shown that transfer from the pigment(s) absorbing around 663 nm to the low energy ones occurs in 5 +/- 1 ps, whereas the 670-nm excitation is delivered to the same "destination" in two phases (0.30 +/- 0.05 ps, and 12 +/- 2 ps) and a fast equilibration (lifetime 0.45 +/- 0.05 ps) takes place within the main absorption band (675-680 nm). From comparison with results from similar time-resolved measurements on trimeric samples, it can be concluded that the intramonomeric energy transfer completely determines the spectral equilibration observed in native LHCII complexes. To correlate the measured lifetimes and their associated spectra with the pigment organization within the available structural model of LHCII (Kuhlbrandt et. al. 1994. Nature. 367:614-621), extensive but straightforward theoretical modeling was used. Thus it is demonstrated that the pigment assignment (Chl a or Chl b) given by Kuhlbrandt and co-workers cannot simultaneously describe the dichroic spectra and the transient absorption results for the rather homologous LHCII and CP29 proteins. A more recent assignment for CP29, in which a Chl b molecule ("Chl b5") is identified as a Chl a (Dr. R. Bassi, personal communication), leads to a much better description of both CP29 and LHCII. Furthermore, the orientations of the transition dipole moments, which have not been obtained in the crystal structure, are now assigned for most of the Chl's.