JBIC Journal of Biological Inorganic Chemistry

, Volume 4, Issue 6, pp 804–813

Variable forms of soluble guanylyl cyclase: protein-ligand interactions and the issue of activation by carbon monoxide

  • Kathleen M. Vogel
  • Songzhou Hu
  • T. G. Spiro
  • Elizabeth A. Dierks
  • Anita E. Yu
  • J. N. Burstyn
ORIGINAL ARTICLE

DOI: 10.1007/s007750050354

Cite this article as:
Vogel, K., Hu, S., Spiro, T. et al. JBIC (1999) 4: 804. doi:10.1007/s007750050354

1

, the resting Fe(II) state is mainly 6-coordinate and low-spin, and the CO adduct has vibrational frequencies characteristic of a histidine-heme-CO complex in a hydrophobic environment. In contrast, the protein sGC2 is 5-coordinate, high-spin in the resting state, and the CO adduct has perturbed vibrational frequencies indicative of a negatively polarizing residue in the binding pocket. The differences may result from the need to reconstitute sGC1 or different isolation procedures for sGC1 versus sGC2. However, both sGC1 and sGC2 are activated by the same mechanism, namely displacement of the proximal histidine ligand upon NO binding, and neither one is activated by CO. If CO is an activator in vivo, some additional molecular component is required.

Soluble guanylyl cyclase Nitric oxide Carbon monoxide Resonance Raman spectroscopy 

Copyright information

© Society of Biological Inorganic Chemistry 1999

Authors and Affiliations

  • Kathleen M. Vogel
    • 1
  • Songzhou Hu
    • 1
  • T. G. Spiro
    • 1
  • Elizabeth A. Dierks
    • 2
  • Anita E. Yu
    • 3
  • J. N. Burstyn
    • 4
  1. 1.Department of Chemistry, Princeton University, Princeton NJ 08544, USA e-mail: spiro@princeton.edu Fax: +1-609-2580348US
  2. 2.Wyeth-Ayerst Research, Drug Metabolism Division, CN800 Princeton, NJ 08543-8000, USAUS
  3. 3.Antex Biologics, Inc., 3000 Professional Drive, Gaithersburg MD 20879, USAUS
  4. 4.Department of Chemistry, University of Wisconsin, Madison WI 53706, USA e-mail: burstyn@chem.wisc.edu Fax: +1-608-2626143US

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