Identification of the proton pathway in bacterial reaction centers: replacement of Asp-M17 and Asp-L210 with asn reduces the proton transfer rate in the presence of Cd2+.

@article{Paddock2000IdentificationOT,
  title={Identification of the proton pathway in bacterial reaction centers: replacement of Asp-M17 and Asp-L210 with asn reduces the proton transfer rate in the presence of Cd2+.},
  author={Mark L. Paddock and Gergely Feh{\'e}r and Melvin Y Okamura},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 4},
  pages={1548-53}
}
The reaction center (RC) from Rhodobacter sphaeroides converts light into chemical energy through the reduction and protonation of a bound quinone molecule Q(B) (the secondary quinone electron acceptor). We investigated the proton transfer pathway by measuring the proton-coupled electron transfer, k(AB)((2)) [Q(A)Q(B) + H(+) --> Q(A)(Q(B)H)(-)] in native and mutant RCs in the absence and presence of Cd(2+). Previous work has shown that the binding of Cd(2+) decreases k(AB)((2)) in native RCs… CONTINUE READING
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