The interplay between heme iron and protein sulfhydryls in the reaction of dimeric Scapharca inaequivalvis hemoglobin with nitric oxide.

@article{Boffi2002TheIB,
  title={The interplay between heme iron and protein sulfhydryls in the reaction of dimeric Scapharca inaequivalvis hemoglobin with nitric oxide.},
  author={A. Boffi and P. Sarti and G. Amiconi and E. Chiancone},
  journal={Biophysical chemistry},
  year={2002},
  volume={98 1-2},
  pages={
          209-16
        }
}
The homodimeric hemoglobin from the mollusk Scapharca inaequivalvis possesses a single reactive cysteine residue per monomer, Cys92, which is located in the subunit interface in the vicinity of the heme group. The interplay between the heme iron and Cys92 towards the reaction with NO has been investigated by the combined use of electrospray mass spectrometry, FTIR and UV-Visible spectroscopy. When the ferrous liganded or unliganded protein reacts with free NO in solution Cys92 is not modified… Expand
Gas-phase spectroscopy of ferric heme-NO complexes.
Regulation of the Monomer-Dimer Equilibrium in Inducible Nitric-oxide Synthase by Nitric Oxide*
Catalytic peroxidation of nitrogen monoxide and peroxynitrite by globins
Ligand-protein interactions in nitric oxide synthase.
Reductive nitrosylation of the cardiolipin‐ferric cytochrome c complex
Reductive nitrosylation of ferric microperoxidase-11
...
1
2
...

References

SHOWING 1-10 OF 26 REFERENCES
Reaction of S-Nitrosoglutathione with the Heme Group of Deoxyhemoglobin*
...
1
2
3
...