The LD spectrum shows a large negative band just above 810 nm, which is due to several overlapping sub-bands. This means that the corresponding transition dipole moments are preferentially oriented along the symmetry axis. The opposite is true for the bands at 805 and Ferrostatin-1 order 825 nm, which exhibit positive LD. On combining these results with the results of polarized fluorescence spectroscopy, an absolute calibration is possible (PF01367338 Wendling et al. 2002). The size of

the LD appears to be in agreement with the orientations of the BChls a in the crystal structure, provided that the Q y transition dipole moment is parallel to the Y-axis in the BChls a. This finding shows that the red-most transition dipole moment of BChl a indeed closely coincides with the Y-axis of the molecule, this is implicitly assumed in many theoretical simulations of the spectroscopic properties of BChl a containing proteins. The absolute calibration of the LD spectrum allowed Wendling et al. (2002) to quantitatively relate the crystal structure to

the LD spectrum, including the precise transition energies (site energies) of all the 7 BChl a pigments (which are influenced by the direct protein environment). Fig. 2 LD spectrum of the FMO (Fenna Matthews Olson) complex from Prosthecochloris aestuarii obtained with a squeezed gel. The spectrum is represented upside down, and the peak at 815 nm indicates that the corresponding transition dipole moments are MK-1775 more or less perpendicular to the C3-symmetry axis of the complex (Vulto et al. 1998a) The FMO complex of Chlorobium tepidum was analyzed N-acetylglucosamine-1-phosphate transferase in a similar way. The spectra are grosso modo quite similar to those of Prosthecochloris aestuarii, and the spectral simulations based on the crystal structure agree even better with the experimental results (Vulto et al. 1998a). The linear-dichroism measurements were not sufficient for the

complete assignment of the site energies and interaction strengths, but they turned out to be crucial. Additional information was obtained from other (polarized) spectroscopic techniques, including CD. Moreover, the pathways of excitation energy transfer and relaxation were studied with transient absorption experiments and could satisfactorily be extracted from the data, using the results of the steady-state (polarized) experiments (Vulto et al. 1998b, 1999). Graham Fleming and coworkers (Brixner et al. 2005), at the University of California at Berkeley, have been able to visualize the flow of excitation energy in the FMO complex using 2D ultrafast spectroscopy. The results were in rather good agreement with those of Thijs Aartsma and coworkers (Vulto et al. 1998b, 1999). It is important to point out, however, that the assignment of the pigment site energies based, amongst others, on the LD experiments, was also essential for the interpretation of the 2D experiments.