The decay kinetics of chlorophyll (Chl) fluorescence of solubilized pigment protein complexes of the distal, proximal, and core antenna of photosystem II from higher plants have been analyzed in the temperature range of 10-277 K using buffer solutions containing or lacking sucrose as cryoprotectant. It was found that (i) at 277 K the (1)Chl* decay of the complexes LHCIIb (distal), CP29 (proximal), and CP47 (core) is characterized by a biphasic kinetics with characteristic lifetimes in the range of 1.5-2.5 ns (fast phase) and 4-4.8 ns (slow phase), (ii) the slow phase dominates in all three complexes with normalized amplitudes of greater than or equal to65, (iii) in solutions containing sucrose the lifetime of the slow phase increases with decreasing temperature and reaches values in the range of 5.2-5.8 ns at 10 K, whereas those of the fast phase exhibit a more complex temperature dependence with a pronounced minimum value in the range of 150-200 K, (iv) markedly different temperature dependencies with pronounced minima in the range of 150-200 K are observed for both lifetime and normalized amplitude of the slow phase when the pigment protein complexes are dissolved in buffers without sucrose. The results are interpreted as evidence for two spectroscopically and kinetically distinguishable subpopulations in solubilized LHCIIb, CP29, and CP47 that are characterized by different rate constants of radiationless decay into the ground state of Chl. Possible mechanisms are discussed.