MOA-STILBENE - A NEW TOOL FOR INVESTIGATION OF THE REACTIONS OF THE CHLOROPLAST CYTOCHROME-BF COMPLEX

MOA-stilbene is known to be a specific inhibitor of the Q(o) site of mammalian cytochrome bc1 complex. We show that it also binds to the chloroplast cytochrome bf complex. Binding to the reduced enzyme induces a red-shift of the Soret and visible absorption bands of the haems b. Steady state and single turnover experiments with thylakoid membranes show that MOA-stilbene promotes additional 'oxidant-induced reduction' of the b haems and slows their subsequent dark reoxidation. In single turnover experiments, the associated slow phase of the carotenoid bandshift at 518 nm is only partially decreased in apparent extent and rate. These and other effects are similar to those produced by NQNO, a Q(i) site effector, and by analogy indicate that MOA-stilbene should also be primarily a Q(i)-site effector of the cytochrome bf complex. MOA-stilbene has less effect on other parts of the photosynthetic chain. This confers an important advantage on MOA-stilbene in that its effects on the cytochrome bf complex can be studied by using Photosystem II to activate turnover. Myxothiazol displays effects on the cytochrome bf complex which are similar to, but much weaker than, those of MOA-stilbene. A Q cycle-based model of turnover of the cytochrome bf complex is presented, which can account for several unusual features of kinetic behaviour.