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

Abstract

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.