Purification and characterization of the Rieske iron-sulfur protein from Thermus thermophilus. Evidence for a [2Fe-2S] cluster having non-cysteine ligands.

@article{Fee1984PurificationAC,
  title={Purification and characterization of the Rieske iron-sulfur protein from Thermus thermophilus. Evidence for a [2Fe-2S] cluster having non-cysteine ligands.},
  author={James A. Fee and K. Findling and Tadashi Yoshida and R. F. Hille and George E. Tarr and David O. Hearshen and William R. Dunham and Edmund P. Day and Thomas A. Kent and Eckard M{\"u}nck},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 1},
  pages={124-33}
}
We have purified the Rieske iron-sulfur protein from Thermus thermophilus. Chemical analyses show that the protein contains iron, labile sulfide, and cysteine in equimolar concentrations, four of each for Mr approximately 20,000. The oxidized and reduced form of the protein have been characterized by optical, EPR, CD, magnetic CD and Mössbauer spectroscopies. Our data suggest the presence of a unique iron-sulfur center. Mössbauer studies of the oxidized and reduced protein demonstrate… CONTINUE READING
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