Protein/Lipid Interaction in the Bacterial Photosynthetic Reaction Center: Phosphatidylcholine and Phosphatidylglycerol Modify the Free Energy Levels of the Quinones.

The role of characteristic phospholipids of native membranes, phosphatidylcholine (PC), phosphatidylglycerol (PG), and cardiolipin (CL), was studied in the energetics of the acceptor quinone side in photosynthetic reaction centers of Rhodobacter sphaeroides. The rates of the first, kAB(1), and the second, kAB(2), electron transfer and that of the charge recombination, kBP, the free energy levels of QA-(B) and QAQB- states, and the changes of charge compensating protein relaxation were determined in RCs incorporated into artificial lipid bilayer membranes. In RCs embedded in the PC vesicle, kAB(1) and kAB(2) increased (from 3100 to 4100 s-1 and from 740 to 3300 s-1, respectively) and kBP decreased (from 0.77 to 0.39 s-1) compared to those measured in detergent at pH 7. In PG, kAB(1) and kBP decreased (to values of 710 and 0.26 s-1, respectively), while kAB(2) increased to 1506 s-1 at pH 7. The free energy between the QA-QB and QAQB- states decreased in PC and PG (δG °QA-QB→QAQB-- = -76.9 and -88.5 meV, respectively) compared to that measured in detergent (-61.8 meV). The changes of the QA/QA- redox potential measured by delayed luminescence showed (1) a differential effect of lipids whether RC incorporated in micelles or vesicles, (2) an altered binding interaction between anionic lipids and RC, (3) a direct influence of PC and PG on the free energy levels of the primary and secondary quinones probably through the intraprotein hydrogen-bonding network, and (4) a larger increase of the QA/QA- free energy in PG than in PC both in detergent micelles and in single-component vesicles. On the basis of recent structural data, implications of the binding properties of phospholipids to RC and possible interactions between lipids and electron transfer components will be discussed. [ABSTRACT FROM AUTHOR]