title: The position of QB in the photosynthetic reaction center depends on pH: a theoretical analysis of the proton uptake upon QB reduction.
abstract: Electrostatics-based calculations have been performed to examine the proton uptake upon reduction of the terminal electron acceptor Q(B) in the photosynthetic reaction center of Rhodobacter sphaeroides as a function of pH and the associated conformational equilibrium. Two crystal structures of the reaction center were considered: one structure was determined in the dark and the other under illumination. In the two structures, the Q(B) was found in two different positions, proximal or distal to the nonheme iron. Because Q(B) was found mainly in the distal position in the dark and only in the proximal position under illumination, the two positions have been attributed mostly to the oxidized and the reduced forms of Q(B), respectively. We calculated the proton uptake upon Q(B) reduction by four different models. In the first model, Q(B) is allowed to equilibrate between the two positions with either oxidation state. This equilibrium was allowed to vary with pH. In the other three models the distribution of Q(B) between the proximal position and the distal position was pH-independent, with Q(B) occupying only the distal position or only the proximal position or populating the two positions with a fixed ratio. Only the first model, which includes the pH-dependent conformational equilibrium, reproduces both the experimentally measured pH dependence of the proton uptake and the crystallographically observed conformational equilibrium at pH 8. From this model, we find that Q(B) occupies only the distal position below pH 6.5 and only the proximal position above pH 9.0 in both oxidation states. Between these pH values both positions are partially occupied. The reduced Q(B) has a higher occupancy in the proximal position than the oxidized Q(B). In summary, the present results indicate that the conformational equilibrium of Q(B) depends not only on the redox state of Q(B), but also on the pH value of the solution.
authors.affiliation: Biocomputing Group, IWR, INF 368, Universität Heidelberg, Germany.
authors.forename: Antoine
authors.initials: A
authors.lastname: Taly
authors.forename: Pierre
authors.initials: P
authors.lastname: Sebban
authors.forename: Jeremy C
authors.initials: JC
authors.lastname: Smith
authors.forename: G Matthias
authors.initials: GM
authors.lastname: Ullmann
mesh_terms: D003198:Computer Simulation; D003461:Crystallography / Q000379:methods*; D004579:Electron Transport; D004735:Energy Transfer; D006863:Hydrogen-Ion Concentration; D008027:Light; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D010084:Oxidation-Reduction; D017785:Photons; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000528:radiation effects*; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides / Q000737:chemistry
chemical_list: D045322:Photosynthetic Reaction Center Complex Proteins