Protein control of the redox potential of the primary quinone acceptor in reactioncCenters from Rhodobacter sphaeroides.

@article{Takahashi2001ProteinCO,
  title={Protein control of the redox potential of the primary quinone acceptor in reactioncCenters from Rhodobacter sphaeroides.},
  author={Eiji Takahashi and Todd A. Wells and Colin A. Wraight},
  journal={Biochemistry},
  year={2001},
  volume={40 4},
  pages={1020-8}
}
The role of the protein environment in determining the redox midpoint potential (E(m)) of Q(A), the primary quinone of bacterial reaction centers, was investigated by mutation of isoleucine at position 265 of the M subunit in Rhodobacter sphaeroides. Isoleucine was changed to threonine, serine, and valine, yielding mutants M265IT, M265IS, and M265IV, respectively. All three mutants, with smaller residues replacing isoleucine, exhibited decreased binding affinities of the Q(A) site for various… CONTINUE READING

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