• Chemistry, Medicine
  • Published in
    The Journal of biological…
    1977

Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c.

@article{Brautigan1977MultipleLS,
  title={Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c.},
  author={David L. Brautigan and Benjamin A. Feinberg and Brian M Hoffman and Emanuel Margoliash and J Preisach and William E. Blumberg},
  journal={The Journal of biological chemistry},
  year={1977},
  volume={252 2},
  pages={
          574-82
        }
}
1. Despite the same methionine-sulfur:heme-iron:imidazole-nitrogen hemochrome structure observed by x-ray crystallography in four of the seven c-type eukaryotic and prokaryotic cytochromes examined, and the occurrence of the characteristic 695 nm absorption band correlated with the presence of a methionine-sulfur:heme-iron axial ligand in all seven proteins, they fall into two distinct classes on the basis of their EPR and optical spectra. The horse, tuna, and bakers' yeast iso-1 cytochromes c… CONTINUE READING

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Engineered holocytochrome c synthases that biosynthesize new cytochromes c.

Deanna L. Mendez, Shalon E. Babbitt, +5 authors Robert G. Kranz
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2017