Energetics of the exchangeable quinone, Q_B, in Photosystem II.

Abstract

Photosystem II (PSII), the light-driven water/plastoquinone photooxidoreductase, is of central importance in the planetary energy cycle. The product of the reaction, plastohydroquinone (PQH₂), is released into the membrane from the Q_B site, where it is formed. A plastoquinone (PQ) from the membrane pool then binds into the Q_B site. Despite their functional importance, the thermodynamic properties of the PQ in the Q_B site, Q_B, in its different redox forms have received relatively little attention. Here we report the midpoint potentials (<i>E_m</i> ) of Q_B in PSII from <i>Thermosynechococcus elongatus</i> using electron paramagnetic resonance (EPR) spectroscopy: <i>E_m</i> Q_B/Q_B^•- ≈ 90 mV, and <i>E_m</i> Q_B^•-/Q_BH₂ ≈ 40 mV. These data allow the following conclusions: 1) The semiquinone, Q_B^•-, is stabilized thermodynamically; 2) the resulting <i>E_m</i> Q_B/Q_BH₂ (∼65 mV) is lower than the <i>E_m</i> PQ/PQH₂ (∼117 mV), and the difference (ΔE ≈ 50 meV) represents the driving force for Q_BH₂ release into the pool; 3) PQ is ∼50× more tightly bound than PQH₂; and 4) the difference between the <i>E_m</i> Q_B/Q_B^•- measured here and the <i>E_m</i> Q_A/Q_A^•- from the literature is ∼234 meV, in principle corresponding to the driving force for electron transfer from Q_A^•- to Q_B The pH dependence of the thermoluminescence associated with Q_B^•- provided a functional estimate for this energy gap and gave a similar value (≥180 meV). These estimates are larger than the generally accepted value (∼70 meV), and this is discussed. The energetics of Q_B in PSII are comparable to those in the homologous purple bacterial reaction center.