Spectral and redox characterization of the heme ci of the cytochrome b6f complex.

@article{Alric2005SpectralAR,
  title={Spectral and redox characterization of the heme ci of the cytochrome b6f complex.},
  author={Jean Alric and Yves St. Pierre and Daniel Picot and J{\'e}r{\^o}me Lavergne and Fabrice Rappaport},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 44},
  pages={15860-5}
}
Absorption spectra of the purified cytochrome b(6)f complex from Chlamydomonas reinhardtii were monitored as a function of the redox potential. Four spectral and redox components were identified: in addition to heme f and the two b hemes, the fourth component must be the new heme c(i) (also denoted x) recently discovered in the crystallographic structures. This heme is covalently attached to the protein, but has no amino acid axial ligand. It is located in the plastoquinone-reducing site Q(i… CONTINUE READING

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