Function of two β-carotenes near the D1 and D2 proteins in photosystem II dimers

The antenna proteins in photosystem II (PSII) not only promote energy transfer to the photosynthetic reaction center (RC) but provide also an efficient cation sink to re-reduce chlorophyll a if the electron transfer (ET) from the Mn-cluster is inhibited. Using the newest PSII dimer crystal structure (3.0 angstrom resolution), in which 11 beta-carotene molecules (Car) and 14 lipids are visible in the PSII monomer, we calculated the redox potentials (E-m) of one-electron oxidation for all Car (E-m(Car)) by solving the Poisson-Boltzmann equation. In each PSII monomer, the D1 protein harbors a previously unlocated Car (Car(D1)) in van der Waals contact with the chlorin ring of Ch1(Z(D1)). Each Car(D1) in the PSII dimer complex is located in the interface between the D1 and CP47 subunits, together with another four Car of the other PSII monomer and several lipid molecules. The proximity of Car bridging between CarD, and plastoquinone/Q(A) may imply a direct charge recombination of Car(+)Q(A)(-). The calculated E-m(Car(D1)) and E-m(Chl(Z(D1))) are, respectively, 83 and 126 mV higher than Em(Car(D2)) and E-m(Chl(Z(D2))), which could explain why Car(D2)(+), and Chl(Z(D2))(+) are observed rather than the corresponding Car(D1)(+) and Chl(Z(D1))(+). (c) 2006 Elsevier B.V. All rights reserved.