Sie. Vulto et al., EXCITED-STATE ENERGY RELAXATION IN THE FMO COMPLEXES OF THE GREEN BACTERIUM PROSTHECOCHLORIS-AESTUARII AT LOW-TEMPERATURES, JOURNAL OF PHYSICAL CHEMISTRY B, 101(24), 1997, pp. 4845-4850
Energy transfer processes at 10 K in the water-soluble bacteriochlorop
hyll a-protein complex (FMO complex) from the green bacterium Prosthec
ochloris aestuarii have been studied by femtosecond one- and two-color
pump-probe measurements. Decay-associated spectra have been obtained
for different excitation wavelengths. From these we conclude that ener
gy relaxation occurs via a stepwise, cascading process down the Q(y) m
anifold of energy states in the FMO complex. Observed time constants f
or these steps are 500 fs and 1.7, 5.5, and 30 ps and are correlated w
ith the position in the Q(y) manifold, becoming shorter with increasin
g energy. Anisotropy decay functions at different wavelengths exhibit
two major components: one of similar to 100 fs and one of similar to 1
ps.