Rewiring photosynthesis: engineering wrong-way electron transfer in the purple bacterial reaction centre.

The purple bacterial reaction centre uses light energy to separate charge across the cytoplasmic membrane, reducing ubiquinone and oxidizing a c-type cytochrome. The protein possesses a macroscopic structural two-fold symmetry but displays a strong functional asymmetry, with only one of two available membrane-spanning branches of cofactors (the so-called A-branch) being used to catalyse photochemical charge separation. The factors underlying this functional asymmetry have been the subject of study for many years but are still not fully understood. Site-directed mutagenesis has been partially successful in rerouting electron transfer along the normally inactive B-branch, allowing comparison of the kinetics of equivalent electron transfer reactions on the two branches. Both the primary and secondary electron transfer steps on the B-branch appear to be considerably slower than their A-branch counterparts. The effectiveness of different mutations in rerouting electron transfer along the B-branch of cofactors is discussed.

Is there a conserved interaction between cardiolipin and the type II bacterial reaction center?

In a recent publication, the structural details of an interaction between the Rhodobacter sphaeroides reaction center and the anionic phospholipid diphosphatidyl glycerol (cardiolipin) were described (K. E. McAuley, P. K. Fyfe, J. P. Ridge, N. W. Isaacs, R. J. Cogdell, and M. R. Jones, 1999, Proc. Natl. Acad. Sci. U.S.A. 96:14706-14711). This was the first crystallographic description of an interaction between this biologically important lipid and an integral membrane protein and was also the first piece of evidence that the reaction center has a specific interaction with cardiolipin. We have examined the extent to which the residues that interact with the cardiolipin are conserved in other species of photosynthetic bacteria with this type of reaction center and discuss the possibility that this cardiolipin binding site is a conserved feature of these reaction centers. We look at how sequence variations that would affect the shape of the cardiolipin binding site might affect the protein-cardiolipin interaction, by modeling the binding of cardiolipin to the reaction center from Rhodopseudomonas viridis.