Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin.

@article{Augustin1983InteractionOC,
  title={Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin.},
  author={M A Augustin and Stephen K. Chapman and Dineh M. Davies and A. Geoffrey Sykes and Samuel H Speck and Emanuel Margoliash},
  journal={The Journal of biological chemistry},
  year={1983},
  volume={258 10},
  pages={6405-9}
}
Bimolecular rate constants have been determined for the reactions of native horse cytochrome c, eight 4-carboxy-2,6-dinitrophenyl (CDNP-) cytochromes c singly modified at lysines 7, 13, 25, 27, 60, 72, 86, or 87 and one 2,3,6-trinitrophenyl cytochrome c singly modified at lysine 13, with the blue copper proteins, plastocyanin (from parsley leaves) and azurin (from Pseudomonas aeruginosa). Plastocyanin, a protein having a negative charge of about -7, yields a bimolecular rate constant with… CONTINUE READING