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To probe the structural elements that contribute to the functional asymmetries of the two ubiquinone10 binding pockets in the reaction center of Rhodobacter capsulatus, we targeted the L212Glu–L213Asp (near QB) and the M246Ala-M247Ala (near QA) pairs of symmetry-related residues for site-specific mutagenesis. We have constructed site-specific mutants that eliminate the sequence differences at these...
Flash-induced absorption spectroscopy has been used to characterize Rhodobacter capsulatus reaction centers mutated in the secondary quinone acceptor site (Q B ). We compared the wild-type, the L212Glu-L213Asp→Ala-Ala photosynthetically incompetent double mutant (DM), and two photocompetent revertants, the DM+L217Arg→Cys and the DM+M5Asn→Asp strains. The electrostatic environment for Q ...
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