Evidence for two Qa-like quinone binding sites in the reaction centre of Rhodopseudomonas viridis

The oxidation-reduction potential of the iron-quinone electron acceptors in the reaction centre of Rhodopseudomonas viridis has been reinvestigated. In chromatophores treated with o-phenanthroline to remove the secondary acceptor Q_b, two steps were observed in the reduction of the primary electron acceptor Q_a with E_m ≈ − 100 and ≈ − 330 mV. In isolated reaction centres only one step was observed in the reduction of Q_a with E ≈ −150 mV. Reconstitution of the reaction centres with additional menaquinone resulted in an increase in the Q_a EPR signal and reconstitution of the low-potential step in the oxidation-reduction titration. Reconstitution with ubiquinone resulted in the recovery of the secondary quinone Q_b. The addition of ubiquinone did not reconstitute the low-potential step of Q_a reduction, or affect the reconstitution of this step by menaquinone. It is concluded that menaquinone can bind to two sites on the reaction centre. Both have properties of the Q_a site but with different pK values. It is unlikely that either is the same as the Q_b site.