We report the observation of two types of changes in fluorescence spectra of LHCII at 4.2 K following intense illumination of the sample with a spectrally narrow laser beam at wavelengths between 678 and 686 nm. Nonspecific changes (burning-wavelength independent) are characterized by two relatively broad bands: a positive one at - 678.7 nm and a negative one at - 680.8 nm. These changes reveal a -1.3-nm blue shift of the distribution of final emitters in LHCII, from 680.3 nm to - 679.0 nm independent of the excitation wavelength. Specific fluorescence changes (burning-wavelength dependent) are characterized by a sharp hole exactly at the burning wavelength, and positive changes directly to the shorter-and longer-wavelength side of the narrow hole. The negative changes are interpreted as zero-phonon holes, while the positive features are assigned to non-photochemical products. In the low-burning intensity experiment, in addition to the zero-phonon holes, we observed also the holes to the longer wavelength of the zero-phonon hole, which were assigned to a sum of phonon and pseudo-phonon side bands. The shapes of these extra holes are identical to the shapes of the holes revealed in the fluorescence line narrowing experiment. On the basis of the low-burning intensity experiment we estimated the upper limit of the electron-phonon coupling strength for LHCII, characterized by a Huang-Rhys factor of 1.5. and K. Gibasiewicz, M. Rutkowski, R. van Grondelle.
The peptide surfactants are amphiphilic peptides which have a hydrophobic tail and a hydrophilic head, and have been reported to stabilize and protect some membrane proteins more effectively than conventional surfactants. The effects of a class of peptide surfactants on the structure and thermal stability of the photosynthetic membrane protein lightharvesting complex II (LHCII) in aqueous media have been investigated. After treatment with the cationic peptide surfactants A6K, V6K2, I5K2 and I5R2, the absorption at 436 nm and 470 nm decreased and the absorption at 500-510 nm and 684-690 nm increased. Moreover, the circular dichroism (CD) signal intensity in the Soret region also decreased significantly, indicating the conformation of some chlorophyll (Chl) a, Chl b, and the xanthophyll molecules distorted upon cationic peptide surfactants treatment. The anionic peptide surfactants A6D and V6D2 had no obvious effect on the absorption and CD spectra. Except for A6D, these peptides all decreased the thermal stability of LHCII, indicating that these peptides may reconstitute protein into a less stable conformation. In addition, the cationic peptide surfactants resulted in LHCII aggregation, as shown by sucrose gradient ultracentrifugation and fluorescence spectra. and S. Liu, Y. Qiu, D.-Y. Yu