Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme.

@article{Burstyn1995StudiesOT,
  title={Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme.},
  author={Judith N. Burstyn and Anita E. Yu and Elizabeth A. Dierks and Barton K Hawkins and John H. Dawson},
  journal={Biochemistry},
  year={1995},
  volume={34 17},
  pages={5896-903}
}
The mechanism of activation of soluble guanylyl cyclase by NO is poorly understood although it is clear that NO interacts with a heme group in the protein via formation of a heme-nitrosyl adduct. The objective of this study is to investigate the coordination environment of the heme in the enzyme spectroscopically in the presence of known heme ligands and to… CONTINUE READING