Skip to main content
Journal cover image

Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes.

Publication ,  Journal Article
Derbyshire, ER; Gunn, A; Ibrahim, M; Spiro, TG; Britt, RD; Marletta, MA
Published in: Biochemistry
March 2008

Soluble guanylate cyclase (sGC), a hemoprotein, is the primary nitric oxide (NO) receptor in higher eukaryotes. The binding of NO to sGC leads to the formation of a five-coordinate ferrous-nitrosyl complex and a several hundred-fold increase in cGMP synthesis. NO activation of sGC is influenced by GTP and the allosteric activators YC-1 and BAY 41-2272. Electron paramagnetic resonance (EPR) spectroscopy shows that the spectrum of the sGC ferrous-nitrosyl complex shifts in the presence of YC-1, BAY 41-2272, or GTP in the presence of excess NO relative to the heme. These molecules shift the EPR signal from one characterized by g 1 = 2.083, g 2 = 2.036, and g 3 = 2.012 to a signal characterized by g 1 = 2.106, g 2 = 2.029, and g 3 = 2.010. The truncated heme domain constructs beta1(1-194) and beta2(1-217) were compared to the full-length enzyme. The EPR spectrum of the beta2(1-217)-NO complex is characterized by g 1 = 2.106, g 2 = 2.025, and g 3 = 2.010, indicating the protein is a good model for the sGC-NO complex in the presence of the activators, while the spectrum of the beta1(1-194)-NO complex resembles the EPR spectrum of sGC in the absence of the activators. Low-temperature resonance Raman spectra of the beta1(1-194)-NO and beta2(1-217)-NO complexes show that the Fe-NO stretching vibration of the beta2(1-217)-NO complex (535 cm (-1)) is significantly different from that of the beta1(1-194)-NO complex (527 cm (-1)). This shows that sGC can adopt different five-coordinate ferrous nitrosyl conformations and suggests that the Fe-NO conformation characterized by this unique EPR signal and Fe-NO stretching vibration represents a highly active sGC state.

Duke Scholars

Published In

Biochemistry

DOI

EISSN

1520-4995

ISSN

0006-2960

Publication Date

March 2008

Volume

47

Issue

12

Start / End Page

3892 / 3899

Related Subject Headings

  • Spectrum Analysis, Raman
  • Solubility
  • Rats
  • Nitric Oxide
  • Heme
  • Guanylate Cyclase
  • Guanosine Triphosphate
  • Ferrous Compounds
  • Electron Spin Resonance Spectroscopy
  • Computer Simulation
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Derbyshire, E. R., Gunn, A., Ibrahim, M., Spiro, T. G., Britt, R. D., & Marletta, M. A. (2008). Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes. Biochemistry, 47(12), 3892–3899. https://doi.org/10.1021/bi7022943
Derbyshire, Emily R., Alexander Gunn, Mohammed Ibrahim, Thomas G. Spiro, R David Britt, and Michael A. Marletta. “Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes.Biochemistry 47, no. 12 (March 2008): 3892–99. https://doi.org/10.1021/bi7022943.
Derbyshire ER, Gunn A, Ibrahim M, Spiro TG, Britt RD, Marletta MA. Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes. Biochemistry. 2008 Mar;47(12):3892–9.
Derbyshire, Emily R., et al. “Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes.Biochemistry, vol. 47, no. 12, Mar. 2008, pp. 3892–99. Epmc, doi:10.1021/bi7022943.
Derbyshire ER, Gunn A, Ibrahim M, Spiro TG, Britt RD, Marletta MA. Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes. Biochemistry. 2008 Mar;47(12):3892–3899.
Journal cover image

Published In

Biochemistry

DOI

EISSN

1520-4995

ISSN

0006-2960

Publication Date

March 2008

Volume

47

Issue

12

Start / End Page

3892 / 3899

Related Subject Headings

  • Spectrum Analysis, Raman
  • Solubility
  • Rats
  • Nitric Oxide
  • Heme
  • Guanylate Cyclase
  • Guanosine Triphosphate
  • Ferrous Compounds
  • Electron Spin Resonance Spectroscopy
  • Computer Simulation