Cyanide-linked dimer-monomer equilibrium of Chromatium vinosum ferric cytochrome c'.

@article{Motie1991CyanidelinkedDE,
  title={Cyanide-linked dimer-monomer equilibrium of Chromatium vinosum ferric cytochrome c'.},
  author={M Motie and Richard J. Kassner and Terry E. Meyer and Michael A. Cusanovich},
  journal={Biochimica et biophysica acta},
  year={1991},
  volume={1076 1},
  pages={
          97-102
        }
}
Cyanide binding to Chromatium vinosum ferricytochrome c' has been studied to further investigate possible allosteric interactions between the subunits of this dimeric protein. Cyanide binding to C. vinosum cytochrome c' appears to be cooperative. However, the cyanide binding reaction is unusual in that the overall affinity of cyanide increases as the concentration of cytochrome c' decreases and that cyanide binding causes the ligated dimer to dissociate to monomers as shown by gel-filtration… CONTINUE READING

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Structural and functional insights into thermally stable cytochrome c′ from a thermophile

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