Picosecond fluorescence of intact and dissolved PSI-LHCI crystals

Over the last years many crystal structures of photosynthetic pigment-protein complexes have been determined, and used extensively to model spectroscopic results obtained on the same proteins in solution. However, the crystal structure is not necessarily identical to the structure of the protein in solution. Here we studied picosecond fluorescence of Photosystem I-Light Harvesting Complex I (PSI-LHCI), a multisubunit pigment protein complex that catalyzes the first steps of photosynthesis. The ultrafast fluorescence of PSI-LHCI crystals is identical to that of dissolved crystals, but differs considerably from most kinetics presented in literature. In contrast to most studies, the present data can be modeled quantitatively with only 2 compartments: PSI core and LHCI. This yields the rate of charge separation from an equilibrated core (22.5+/-2.5 ps) and rates of excitation energy transfer from LHCI to core (kLC) and vice versa (kCL). The ratio R=kCL/kLC between these rates appears to be wavelength-dependent and scales with the ratio of the absorption spectra of LHCI and core, indicating the validity of a detailed balance relation between both compartments. kLC depends slightly but non systematically on detection wavelength, averaging (9.4+/-4.9 ps)(-1). R ranges from 0.5 (below 690 nm) to around 1.3 above 720 nm.