Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron-chlorin prosthetic group.

@article{Andersson1984SulfmyoglobinRR,
  title={Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron-chlorin prosthetic group.},
  author={Lars A. A. Andersson and Thomas M. Loehr and Amy Lim and A. Grant Mauk},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 24},
  pages={15340-9}
}
The green heme protein sulfmyoglobin (SMb) has been suggested to contain a sulfur-modified iron chlorin prosthetic group. To evaluate this hypothesis, we have obtained high-frequency (greater than 1000 cm-1) resonance Raman spectra of both oxidized and reduced SMb with 457.9-, 488.0-, 514.5-, 568.2-, and 647.1-nm excitation. The SMb spectra are compared to those of native met- and deoxymyoglobin (Mb). Vibrational frequencies for SMb are generally similar to those of Mb, suggesting a high-spin… CONTINUE READING