Induced conformational changes upon Cd2+ binding at photosynthetic reaction centers.
Cd(2+) binding at the bacterial photosynthetic reaction center (bRC) from Rhodobacter sphaeroides is known to inhibit proton transfer (PT) from bulk solvent to the secondary quinone Q(B). To elucidate this mechanism, we calculated the pK(a) for residues along the water channels connecting Q(B) with the stromal side based on the crystal structures of WT-bRC and Cd(2+)-bound bRC. Upon Cd(2+) binding, we observed the release of two protons from His-H126/128 at the Cd(2+) binding site and significant pK(a) shifts for residues along the PT pathways. Remarkably, Asp-L213 near Q(B), which is proposed to play a significant role in PT, resulted in a decrease in pK(a) upon Cd(2+) binding. The direct electrostatic influence of the Cd(2+)-positive charge on these pK(a) shifts was small. Instead, conformational changes of amino acid side chains induced electrostatically by Cd(2+) binding were the main mechanism for these pK(a) shifts. The long-range electrostatic influence over approximately 12 A between Cd(2+) and Asp-L213 is likely to originate from a set of Cd(2+)-induced successive reorientations of side chains (Asp-H124, His-H126, His-H128, Asp-H170, Glu-H173, Asp-M17, and Asp-L210), which propagate along the PT pathways as a "domino" effect.
Ishikita
Hiroshi
H
Institute of Chemistry and Biochemistry, Free University of Berlin, Takustrasse 6, D-14195 Berlin, Germany.
Knapp
Ernst-Walter
EW
D001665:Binding Sites; D002104:Cadmium / Q000378:metabolism*; D007700:Kinetics; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D055672:Static Electricity
D045322:Photosynthetic Reaction Center Complex Proteins; D002104:Cadmium