Structure and function of the myoglobin containing octaethylhemin as a prosthetic group.

@article{Neya1988StructureAF,
  title={Structure and function of the myoglobin containing octaethylhemin as a prosthetic group.},
  author={Saburo Neya and Noriaki Funasaki and Kiyohiro Imai},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 18},
  pages={8810-5}
}
Spectrophotometric titration of ferric octaethylporphyrin (OEP) with apomyoglobin revealed their 1:1 complex formation. Proton NMR spectrum of the OEP-reconstituted deoxymyoglobin exhibits an exchangeable peak from the proximal F8 histidine at 78.5 ppm, indicating the incorporation of iron OEP into the heme cavity to form the Fe-N(His-F8) bond. OEP… CONTINUE READING