Light harvesting in photosystem II core complexes is limited by the transfer to the trap: can the core complex turn into a photoprotective mode?
A structure-based modeling and analysis of the primary photophysical reactions in photosystem II (PS-II) core complexes is presented. The modeling is based on a description of stationary and time-resolved optical spectra of the CP43, CP47, and D1-D2-cytb559 subunits and whole core complexes. It shows that the decay of excited states in PS-II core complexes with functional (open) reaction centers (RCs) is limited by the excitation energy transfer from the CP43 and CP47 core antennae to the RC occurring with a time constant of 40-50 ps at room temperature. The chlorophylls responsible for the low energy absorbance bands in the CP43 and CP47 subunits are assigned, and their signatures in hole burning, fluorescence line narrowing, and triplet-minus-singlet spectra are explained. The different locations of these trap states in the CP43 and CP47 antennae with respect to the reaction center lead to a dramatic change of the transfer dynamics at low temperatures. The calculations predict that, compared to room temperature, the fluorescence decay at 77 K should reveal a faster transfer from CP43 and a much slower and highly dispersive transfer from CP47 to the RC. A factor of 3 increase in the fastest decay time constant of fluorescence that was reported to occur when the RC is closed (the plastoquinone QA is reduced) is understood in the present model by assuming that the intrinsic rate constant for primary electron transfer decreases from 100 fs-1 for open RCs to 6 ps-1 for closed RCs, leading to a reduction of the primary electron acceptor PheoD1, in 300 fs and 18 ps, respectively. The model suggests that the reduced QA switches the photosystem into a photoprotective mode in which a large part of the excitation energy of the RC returns to the CP43 and CP47 core antennae, where the physiologically dangerous triplet energy of the chlorophylls can be quenched by the carotenoids. Experiments are suggested to test this hypothesis. The ultrafast primary electron transfer inferred for open RCs provides further support for the accessory chlorophyll ChlD1 to be the primary electron donor in photosystem II.
Raszewski
Grzegorz
G
Institut für Chemie und Biochemie (Kristallographie), Freie Universität Berlin, Fabeckstrasse 36a, 6, D-14195 Berlin, Germany.
Renger
Thomas
T
D004579:Electron Transport; D005453:Fluorescence; D008027:Light; D008954:Models, Biological; D008968:Molecular Conformation; D010777:Photochemistry; D045332:Photosystem II Protein Complex / Q000737:chemistry* / Q000528:radiation effects*; D013997:Time Factors
D045332:Photosystem II Protein Complex